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131 hits found for sans

SASDN52SANS data from cytochrome c' from Alcaligenes xylosoxidans at pD = 1.7

Cytochrome c' experimental SAS data
Cytochrome c' Kratky plot
Sample: Cytochrome c' monomer, 14 kDa Achromobacter xylosoxidans protein
Buffer: Phosphate Buffer pD 1.7, pH: 1.7
Experiment: SANS data collected at KWS1, FRM2 on 2017 Aug 12
Open-Bundle Structure as the Unfolding Intermediate of Cytochrome c′ Revealed by Small Angle Neutron Scattering Biomolecules 12(1):95 (2022)
Yamaguchi T, Akao K, Koutsioubas A, Frielinghaus H, Kohzuma T
RgGuinier 2.3 nm
Dmax 8.6 nm
VolumePorod 13 nm3

SASDN62SANS data from cytochrome c' from Alcaligenes xylosoxidans at pD = 6.4

Cytochrome c' experimental SAS data
Cytochrome c' Kratky plot
Sample: Cytochrome c' dimer, 27 kDa Alcaligenes protein
Buffer: Phosphate Buffer pD 6.4, pH: 6.4
Experiment: SANS data collected at KWS1, FRM2 on 2017 Aug 12
Open-Bundle Structure as the Unfolding Intermediate of Cytochrome c′ Revealed by Small Angle Neutron Scattering Biomolecules 12(1):95 (2022)
Yamaguchi T, Akao K, Koutsioubas A, Frielinghaus H, Kohzuma T
RgGuinier 1.8 nm
Dmax 5.5 nm
VolumePorod 11 nm3

SASDN72SANS data from cytochrome c' from Alcaligenes xylosoxidans at pD = 9.6

Cytochrome c' experimental SAS data
Cytochrome c' Kratky plot
Sample: Cytochrome c' dimer, 27 kDa Alcaligenes protein
Buffer: Phosphate Buffer pD 9.6, pH: 9.6
Experiment: SANS data collected at KWS1, FRM2 on 2017 Aug 12
Open-Bundle Structure as the Unfolding Intermediate of Cytochrome c′ Revealed by Small Angle Neutron Scattering Biomolecules 12(1):95 (2022)
Yamaguchi T, Akao K, Koutsioubas A, Frielinghaus H, Kohzuma T
RgGuinier 1.9 nm
Dmax 5.3 nm
VolumePorod 10 nm3

SASDN82SANS data from cytochrome c' from Alcaligenes xylosoxidans at pD = 13

Cytochrome c' experimental SAS data
Cytochrome c' Kratky plot
Sample: Cytochrome c' monomer, 14 kDa Achromobacter xylosoxidans protein
Buffer: Phosphate Buffer pD 13, pH: 13
Experiment: SANS data collected at KWS1, FRM2 on 2017 Aug 12
Open-Bundle Structure as the Unfolding Intermediate of Cytochrome c′ Revealed by Small Angle Neutron Scattering Biomolecules 12(1):95 (2022)
Yamaguchi T, Akao K, Koutsioubas A, Frielinghaus H, Kohzuma T
RgGuinier 4.8 nm
Dmax 9.0 nm
VolumePorod 20 nm3

SASDNK2 – ...SANS in 100% D2O

75% deuterated Circadian clock protein KaiBCircadian clock protein KaiA75% deuterated Circadian clock protein kinase KaiC (S431D mutant) experimental SAS data
OTHER model
Sample: 75% deuterated Circadian clock protein KaiB hexamer, 71 kDa Synechococcus elongatus (strain … protein
Circadian clock protein KaiA dodecamer, 393 kDa Synechococcus elongatus (strain … protein
75% deuterated Circadian clock protein kinase KaiC (S431D mutant) hexamer, 357 kDa Synechococcus elongatus (strain … protein
Buffer: 50 mM sodium phosphate buffer, 150 mm NaCl, 5 mM MgCl2, 0.5 mM EDTA, 1 mM ATP, 1 mM DTT, 50 mM arginine, 50 mM glutamine, in 100% D2O, pH: 7.8
Experiment: SANS data collected at D22, ILL on 2018 Sep 19
Overall structure of fully assembled cyanobacterial KaiABC circadian clock complex by an integrated experimental-computational approach. Commun Biol 5(1):184 (2022)
Yunoki Y, Matsumoto A, Morishima K, Martel A, Porcar L, Sato N, Yogo R, Tominaga T, Inoue R, Yagi-Utsumi M, Okuda A, Shimizu M, Urade R, Terauchi K, Kono H, Yagi H, Kato K, Sugiyama M
RgGuinier 7.8 nm
Dmax 25.6 nm
VolumePorod 1620 nm3

SASDMU2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) without Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) without Dox experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) without Dox monomer, 125 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III on 2012 Aug 19
...SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
Filippov SK, Franklin JM, Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 6.1 nm
Dmax 20.5 nm

SASDGV2 – ...SANS data in 42% v/v D2O)

Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase50S ribosomal protein L7AeNOP5/NOP56 related proteinpyrococcus furiosus sR26 stabilized constructPyrococcus furiosus sR26 substrate D' experimental SAS data
Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase 50S ribosomal protein L7Ae NOP5/NOP56 related protein pyrococcus furiosus sR26 stabilized construct Pyrococcus furiosus sR26 substrate D' Kratky plot
Sample: Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein
50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein
NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein
pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA
Pyrococcus furiosus sR26 substrate D' monomer, 4 kDa Pyrococcus furiosus RNA
Buffer: 50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment: SANS data collected at KWS1, FRM2 on 2015 May 24
The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T
RgGuinier 4.9 nm
Dmax 16.0 nm
VolumePorod 87 nm3

SASDMV2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) with Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) with Dox (10%) experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) with Dox (10%) monomer, 220 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III on 2012 Aug 19
...SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
Filippov SK, Franklin JM, Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 7.5 nm
Dmax 25.5 nm

SASDGW2 – ...SANS data in 42% v/v D2O)

Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase50S ribosomal protein L7AeNOP5/NOP56 related proteinpyrococcus furiosus sR26 stabilized constructPyrococcus furiosus sR26 substrate D' experimental SAS data
Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase 50S ribosomal protein L7Ae NOP5/NOP56 related protein pyrococcus furiosus sR26 stabilized construct Pyrococcus furiosus sR26 substrate D' Kratky plot
Sample: Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein
50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein
NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein
pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA
Pyrococcus furiosus sR26 substrate D' monomer, 4 kDa Pyrococcus furiosus RNA
Buffer: 50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment: SANS data collected at D22, ILL on 2015 Sep 21
The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T
RgGuinier 4.1 nm
Dmax 14.0 nm
VolumePorod 210 nm3

SASDMW2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) without Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) without Dox experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) without Dox monomer, 125 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III on 2012 Aug 19
...SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
Filippov SK, Franklin JM, Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 6.4 nm
Dmax 22.5 nm

SASDGX2 – ...SANS data in 42% v/v D2O)

Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase50S ribosomal protein L7AeNOP5/NOP56 related proteinpyrococcus furiosus sR26 stabilized constructPyrococcus furiosus sR26 substrate D' experimental SAS data
Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase 50S ribosomal protein L7Ae NOP5/NOP56 related protein pyrococcus furiosus sR26 stabilized construct Pyrococcus furiosus sR26 substrate D' Kratky plot
Sample: Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein
50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein
NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein
pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA
Pyrococcus furiosus sR26 substrate D' monomer, 4 kDa Pyrococcus furiosus RNA
Buffer: 50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment: SANS data collected at D22, ILL on 2015 Nov 23
The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T
RgGuinier 4.0 nm
Dmax 13.3 nm
VolumePorod 42 nm3

SASDMX2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) with Dox (10%)

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) with Dox (10%) experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) with Dox (10%) monomer, 225 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III on 2012 Aug 19
...SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
Filippov SK, Franklin JM, Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 10.0 nm
Dmax 21.9 nm

SASDGY2 – ...SANS data in 42% v/v D2O)

Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase50S ribosomal protein L7AeNOP5/NOP56 related proteinpyrococcus furiosus sR26 stabilized constructPyrococcus furiosus sR26 substrate D' experimental SAS data
Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase 50S ribosomal protein L7Ae NOP5/NOP56 related protein pyrococcus furiosus sR26 stabilized construct Pyrococcus furiosus sR26 substrate D' Kratky plot
Sample: Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein
50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein
NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein
pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA
Pyrococcus furiosus sR26 substrate D' monomer, 4 kDa Pyrococcus furiosus RNA
Buffer: 50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment: SANS data collected at D22, ILL on 2019 Jul 21
The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T
RgGuinier 2.8 nm
Dmax 9.9 nm
VolumePorod 52 nm3

SASDMY2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) without Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) without Dox experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) without Dox monomer, 125 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III on 2012 Aug 19
...SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
Filippov SK, Franklin JM, Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 6.5 nm
Dmax 22.9 nm

SASDGZ2 – ...SANS data in 42% v/v D2O)

Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase50S ribosomal protein L7AeNOP5/NOP56 related proteinpyrococcus furiosus sR26 stabilized constructPyrococcus furiosus sR26 substrate D' experimental SAS data
Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase 50S ribosomal protein L7Ae NOP5/NOP56 related protein pyrococcus furiosus sR26 stabilized construct Pyrococcus furiosus sR26 substrate D' Kratky plot
Sample: Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein
50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein
NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein
pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA
Pyrococcus furiosus sR26 substrate D' monomer, 4 kDa Pyrococcus furiosus RNA
Buffer: 50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment: SANS data collected at KWS1, FRM2 on 2015 May 23
The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T
RgGuinier 4.8 nm
Dmax 16.6 nm
VolumePorod 82 nm3

SASDMZ2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) with Dox (10%)

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) with Dox (10%) experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) with Dox (10%) monomer, 125 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III on 2012 Aug 19
...SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
Filippov SK, Franklin JM, Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 6.9 nm
Dmax 23.8 nm

SASDG23 – ...SANS data in 42% v/v D2O)

Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase50S ribosomal protein L7AeNOP5/NOP56 related proteinpyrococcus furiosus sR26 stabilized constructPyrococcus furiosus sR26 substrate D' experimental SAS data
Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase 50S ribosomal protein L7Ae NOP5/NOP56 related protein pyrococcus furiosus sR26 stabilized construct Pyrococcus furiosus sR26 substrate D' Kratky plot
Sample: Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein
50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein
NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein
pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA
Pyrococcus furiosus sR26 substrate D' monomer, 4 kDa Pyrococcus furiosus RNA
Buffer: 50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment: SANS data collected at D22, ILL on 2018 Apr 8
The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T
RgGuinier 4.0 nm
Dmax 13.8 nm
VolumePorod 214 nm3

SASDM23 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) without Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) without Dox experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) without Dox monomer, 125 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III on 2012 Aug 16
...SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
Filippov SK, Franklin JM, Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 5.9 nm
Dmax 19.7 nm

SASDG33 – ...SANS data in 42% v/v D2O)

Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase50S ribosomal protein L7AeNOP5/NOP56 related proteinpyrococcus furiosus sR26 stabilized constructPyrococcus furiosus sR26 substrate D experimental SAS data
Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase 50S ribosomal protein L7Ae NOP5/NOP56 related protein pyrococcus furiosus sR26 stabilized construct Pyrococcus furiosus sR26 substrate D Kratky plot
Sample: Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein
50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein
NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein
pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA
Pyrococcus furiosus sR26 substrate D monomer, 4 kDa Pyrococcus furiosus RNA
Buffer: 50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment: SANS data collected at D22, ILL on 2018 Apr 8
The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T
RgGuinier 4.0 nm
Dmax 13.9 nm
VolumePorod 231 nm3

SASDL33 – ...SANS

Proton-gated ion channel experimental SAS data
GROMACS model
Sample: Proton-gated ion channel pentamer, 183 kDa Gloeobacter violaceus (strain … protein
Buffer: D2O, 20 mM Tris, 150 mM NaCl, 0.5 mM matched-out deuterated DDM,, pH: 7.5
Experiment: SANS data collected at D22, ILL on 2020 Aug 22
Probing solution structure of the pentameric ligand-gated ion channel GLIC by small-angle neutron scattering Proceedings of the National Academy of Sciences 118(37):e2108006118 (2021)
Lycksell M, Rovšnik U, Bergh C, Johansen N, Martel A, Porcar L, Arleth L, Howard R, Lindahl E
RgGuinier 3.8 nm
Dmax 13.5 nm
VolumePorod 274 nm3

SASDM33 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) with Dox (10%)

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) with Dox (10%) experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) with Dox (10%) monomer, 125 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III on 2012 Aug 19
...SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
Filippov SK, Franklin JM, Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 5.5 nm
Dmax 18.3 nm

SASDG43 – ...SANS data in 42% v/v D2O)

Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase50S ribosomal protein L7AeNOP5/NOP56 related proteinpyrococcus furiosus sR26 stabilized constructPyrococcus furiosus sR26 substrate D experimental SAS data
Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase 50S ribosomal protein L7Ae NOP5/NOP56 related protein pyrococcus furiosus sR26 stabilized construct Pyrococcus furiosus sR26 substrate D Kratky plot
Sample: Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein
50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein
NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein
pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA
Pyrococcus furiosus sR26 substrate D monomer, 4 kDa Pyrococcus furiosus RNA
Buffer: 50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment: SANS data collected at KWS1, FRM2 on 2015 May 24
The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T
RgGuinier 4.9 nm
Dmax 16.6 nm
VolumePorod 65 nm3

SASDL43 – ...SANS

Proton-gated ion channel experimental SAS data
GROMACS model
Sample: Proton-gated ion channel pentamer, 183 kDa Gloeobacter violaceus (strain … protein
Buffer: D2O, 20 mM citrate, 150 mM NaCl, 0.5 mM match-out deuterated DDM, pH: 3
Experiment: SANS data collected at D22, ILL on 2020 Aug 22
Probing solution structure of the pentameric ligand-gated ion channel GLIC by small-angle neutron scattering Proceedings of the National Academy of Sciences 118(37):e2108006118 (2021)
Lycksell M, Rovšnik U, Bergh C, Johansen N, Martel A, Porcar L, Arleth L, Howard R, Lindahl E
RgGuinier 3.8 nm
Dmax 12.7 nm
VolumePorod 279 nm3

SASDG53 – ...SANS data in 42% v/v D2O)

Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase50S ribosomal protein L7AeNOP5/NOP56 related proteinpyrococcus furiosus sR26 stabilized constructPyrococcus furiosus sR26 substrate D experimental SAS data
Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase 50S ribosomal protein L7Ae NOP5/NOP56 related protein pyrococcus furiosus sR26 stabilized construct Pyrococcus furiosus sR26 substrate D Kratky plot
Sample: Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein
50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein
NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein
pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA
Pyrococcus furiosus sR26 substrate D monomer, 4 kDa Pyrococcus furiosus RNA
Buffer: 50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment: SANS data collected at D22, ILL on 2015 Sep 21
The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T
RgGuinier 4.1 nm
Dmax 14.0 nm
VolumePorod 222 nm3

SASDL53 – ...SANS

Proton-gated ion channel experimental SAS data
Proton-gated ion channel Kratky plot
Sample: Proton-gated ion channel pentamer, 183 kDa Gloeobacter violaceus (strain … protein
Buffer: D2O, 20 mM Tris, 150 mM NaCl, 0.5 mM matched-out deuterated DDM,, pH: 7.5
Experiment: SANS data collected at D22, ILL on 2019 Jun 20
Probing solution structure of the pentameric ligand-gated ion channel GLIC by small-angle neutron scattering Proceedings of the National Academy of Sciences 118(37):e2108006118 (2021)
Lycksell M, Rovšnik U, Bergh C, Johansen N, Martel A, Porcar L, Arleth L, Howard R, Lindahl E
RgGuinier 3.8 nm
Dmax 12.0 nm
VolumePorod 235 nm3

SASDG63 – ...SANS data in 42% v/v D2O)

Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase50S ribosomal protein L7AeNOP5/NOP56 related proteinpyrococcus furiosus sR26 stabilized constructPyrococcus furiosus sR26 substrate D experimental SAS data
Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase 50S ribosomal protein L7Ae NOP5/NOP56 related protein pyrococcus furiosus sR26 stabilized construct Pyrococcus furiosus sR26 substrate D Kratky plot
Sample: Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein
50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein
NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein
pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA
Pyrococcus furiosus sR26 substrate D monomer, 4 kDa Pyrococcus furiosus RNA
Buffer: 50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment: SANS data collected at D22, ILL on 2015 Nov 23
The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T
RgGuinier 3.9 nm
Dmax 12.5 nm
VolumePorod 49 nm3

SASDJ63 – Streptococcus pneumoniae NADPH oxidase - Tag-free SpNOX

FAD-binding FR-type domain-containing protein experimental SAS data
OTHER model
Sample: FAD-binding FR-type domain-containing protein monomer, 47 kDa Streptococcus pneumoniae protein
Buffer: 50 mM Tris-HCl pH 7, 300 mM NaCl, 5 mM LMNG, 10 µM FAD, 21.4% D₂O, pH: 7
Experiment: SANS data collected at D22, ILL on 2018 Jun 26
...SANS Using LMNG Stealth Carrier. Biophys J 119(3):605-618 (2020)
Vermot A, Petit-Härtlein I, Breyton C, Le Roy A, Thépaut M, Vivès C, Moulin M, Härtlein M, Grudinin S, Smith SME, Ebel C, Martel A, Fieschi F
RgGuinier 3.0 nm
Dmax 10.0 nm
VolumePorod 89 nm3

SASDL63 – ...SANS

Proton-gated ion channel experimental SAS data
Proton-gated ion channel Kratky plot
Sample: Proton-gated ion channel pentamer, 183 kDa Gloeobacter violaceus (strain … protein
Buffer: D2O, 20 mM Tris, 150 mM NaCl, 0.5 mM matched-out deuterated DDM,, pH: 7.5
Experiment: SANS data collected at D22, ILL on 2019 Jun 21
Probing solution structure of the pentameric ligand-gated ion channel GLIC by small-angle neutron scattering Proceedings of the National Academy of Sciences 118(37):e2108006118 (2021)
Lycksell M, Rovšnik U, Bergh C, Johansen N, Martel A, Porcar L, Arleth L, Howard R, Lindahl E
RgGuinier 4.0 nm
Dmax 17.7 nm
VolumePorod 225 nm3

SASDG73 – ...SANS data in 42% v/v D2O)

Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase50S ribosomal protein L7AeNOP5/NOP56 related proteinpyrococcus furiosus sR26 stabilized constructPyrococcus furiosus sR26 substrate D experimental SAS data
Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase 50S ribosomal protein L7Ae NOP5/NOP56 related protein pyrococcus furiosus sR26 stabilized construct Pyrococcus furiosus sR26 substrate D Kratky plot
Sample: Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein
50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein
NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein
pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA
Pyrococcus furiosus sR26 substrate D monomer, 4 kDa Pyrococcus furiosus RNA
Buffer: 50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment: SANS data collected at D22, ILL on 2019 Jul 21
The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T
RgGuinier 2.7 nm
Dmax 9.5 nm
VolumePorod 25 nm3

SASDG83 – ...SANS data in 42% v/v D2O)

Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase50S ribosomal protein L7AeNOP5/NOP56 related proteinpyrococcus furiosus sR26 stabilized constructPyrococcus furiosus sR26 substrate D experimental SAS data
Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase 50S ribosomal protein L7Ae NOP5/NOP56 related protein pyrococcus furiosus sR26 stabilized construct Pyrococcus furiosus sR26 substrate D Kratky plot
Sample: Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein
50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein
NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein
pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA
Pyrococcus furiosus sR26 substrate D monomer, 4 kDa Pyrococcus furiosus RNA
Buffer: 50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment: SANS data collected at KWS1, FRM2 on 2015 May 23
The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T
RgGuinier 5.1 nm
Dmax 15.5 nm
VolumePorod 125 nm3

SASDFL3 – All 1H histone acetyltransferase Rtt109 complex with histones H3 and H4 and histone chaperones Asf1 and Vps75 (acquired in 100% v/v D2O)

Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Mar 3
Histone chaperone exploits intrinsic disorder to switch acetylation specificity. Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 3.5 nm
Dmax 11.8 nm

SASDFM3 – Complex with 1H histone chaperone Asf1 and histones H3 and H4, 2H histone acetyltransferase Rtt109 and histone chaperone Vps75 (1H Asf1-H3:H4, 2H Rtt109-Vps75) acquired in 100% v/v D2O

Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Mar 4
Histone chaperone exploits intrinsic disorder to switch acetylation specificity. Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier -2.8 nm

SASDFN3 – Complex with 1H histone chaperones Asf1 and Vps75 and histones H3 and H4, 70%-2H histone acetyltransferase Rtt109 (1H Asf1-H3:H4-Vps75, 2H(70%) Rtt109) acquired in 100% v/v D2O

Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Mar 4
Histone chaperone exploits intrinsic disorder to switch acetylation specificity. Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 3.3 nm
Dmax 10.5 nm

SASDFQ3 – Complex with 1H histone acetyltransferase Rtt109 and histones H3 and H4, 2H histone chaperones Asf1 and Vps75 (1H Rtt109-H3:H4, 2H Asf1-Vps75) acquired in 42% v/v D2O

Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Mar 5
Histone chaperone exploits intrinsic disorder to switch acetylation specificity. Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 3.5 nm
Dmax 11.0 nm

SASDFR3 – Complex with 1H histone chaperone Vps75 and histones H3 and H4, 2H histone acetyltransferase Rtt109 and histone chaperone Asf1 (1H Vps75-H3:H4, 2H Rtt109-Asf1) acquired in 42% v/v D2O

Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Mar 5
Histone chaperone exploits intrinsic disorder to switch acetylation specificity. Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 3.1 nm
Dmax 10.5 nm

SASDES4 – ...SANS, 100% D2O)

Membrane scaffold protein 1D1 (deuterated, 75%)1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl)Calcium-transporting ATPase 8, plasma membrane-type experimental SAS data
Membrane scaffold protein 1D1 (deuterated, 75%) 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) Calcium-transporting ATPase 8, plasma membrane-type Kratky plot
Sample: Membrane scaffold protein 1D1 (deuterated, 75%) dimer, 49 kDa protein
1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) , 1 kDa Escherichia coli
Calcium-transporting ATPase 8, plasma membrane-type monomer, 118 kDa Arabidopsis thaliana protein
Buffer: 30 mM Tris, 150 mM NaCl, 1mM MgCl2, 1 mM CaCl2, pH: 7.5
Experiment: SANS data collected at SANS-1, Heinz Maier-Leibnitz Zentrum on 2017 Aug 28
Structural basis for activation of plasma-membrane Ca2+-ATPase by calmodulin. Commun Biol 1:206 (2018)
Nitsche J, Josts I, Heidemann J, Mertens HD, Maric S, Moulin M, Haertlein M, Busch S, Forsyth VT, Svergun DI, Uetrecht C, Tidow H
RgGuinier 4.0 nm
Dmax 13.0 nm
VolumePorod 202 nm3

SASDDT4 – Fc region of Immunoglobulin G1 (IgG1 Fc)

Immunoglobulin heavy constant gamma 1 experimental SAS data
BILBOMD model
Sample: Immunoglobulin heavy constant gamma 1 dimer, 53 kDa Homo sapiens protein
Buffer: 20mM HEPES, 50mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Feb 17
Conformational Plasticity of the Immunoglobulin Fc Domain in Solution. Structure 26(7):1007-1014.e2 (2018)
Remesh SG, Armstrong AA, Mahan AD, Luo J, Hammel M
RgGuinier 2.6 nm
Dmax 10.0 nm
VolumePorod 70 nm3

SASDET4 – ...SANS, 100% D2O)

Membrane scaffold protein 1D1 (deuterated, 75%)1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl)Calcium-transporting ATPase 8, plasma membrane-typeCalmodulin-7 (deuterated 75%) experimental SAS data
ACA8 complex with Calmodulin (75% deuterated) in stealth nanodisc (SANS, 100% D2O) Rg histogram
Sample: Membrane scaffold protein 1D1 (deuterated, 75%) dimer, 49 kDa protein
1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) , 1 kDa Escherichia coli
Calcium-transporting ATPase 8, plasma membrane-type monomer, 118 kDa Arabidopsis thaliana protein
Calmodulin-7 (deuterated 75%) monomer, Arabidopsis thaliana protein
Buffer: 30 mM Tris, 150 mM NaCl, 1mM MgCl2, 1 mM CaCl2, pH: 7.5
Experiment: SANS data collected at SANS-1, Heinz Maier-Leibnitz Zentrum on 2017 Aug 28
Structural basis for activation of plasma-membrane Ca2+-ATPase by calmodulin. Commun Biol 1:206 (2018)
Nitsche J, Josts I, Heidemann J, Mertens HD, Maric S, Moulin M, Haertlein M, Busch S, Forsyth VT, Svergun DI, Uetrecht C, Tidow H
RgGuinier 4.3 nm
Dmax 15.0 nm
VolumePorod 217 nm3

SASDDU4 – Fc region of Immunoglobulin G2 (IgG2 Fc)

Immunoglobulin heavy constant gamma 2 experimental SAS data
BILBOMD model
Sample: Immunoglobulin heavy constant gamma 2 dimer, 52 kDa Homo sapiens protein
Buffer: 20mM HEPES, 50mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Feb 17
Conformational Plasticity of the Immunoglobulin Fc Domain in Solution. Structure 26(7):1007-1014.e2 (2018)
Remesh SG, Armstrong AA, Mahan AD, Luo J, Hammel M
RgGuinier 2.8 nm
Dmax 9.0 nm
VolumePorod 67 nm3

SASDEU4 – ...SANS, 100% D2O)

Membrane scaffold protein 1D1 (deuterated, 75%)1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl)Calcium-transporting ATPase 8, plasma membrane-typeCalmodulin-7 experimental SAS data
Membrane scaffold protein 1D1 (deuterated, 75%) 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) Calcium-transporting ATPase 8, plasma membrane-type Calmodulin-7 Kratky plot
Sample: Membrane scaffold protein 1D1 (deuterated, 75%) dimer, 49 kDa protein
1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) , 1 kDa Escherichia coli
Calcium-transporting ATPase 8, plasma membrane-type monomer, 118 kDa Arabidopsis thaliana protein
Calmodulin-7 monomer, Arabidopsis thaliana protein
Buffer: 30 mM Tris, 150 mM NaCl, 1mM MgCl2, 1 mM CaCl2, pH: 7.5
Experiment: SANS data collected at SANS-1, Heinz Maier-Leibnitz Zentrum on 2017 Aug 28
Structural basis for activation of plasma-membrane Ca2+-ATPase by calmodulin. Commun Biol 1:206 (2018)
Nitsche J, Josts I, Heidemann J, Mertens HD, Maric S, Moulin M, Haertlein M, Busch S, Forsyth VT, Svergun DI, Uetrecht C, Tidow H
RgGuinier 4.8 nm
Dmax 18.0 nm
VolumePorod 297 nm3

SASDDV4 – Fc-region of Immunoglobulin G1, M135Y/S137T/T139E mutant (IgG1 Fc-YTE)

Immunoglobulin heavy constant gamma 1 M255Y/S257T/T259E experimental SAS data
BILBOMD model
Sample: Immunoglobulin heavy constant gamma 1 M255Y/S257T/T259E dimer, 53 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 50mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Feb 17
Conformational Plasticity of the Immunoglobulin Fc Domain in Solution. Structure 26(7):1007-1014.e2 (2018)
Remesh SG, Armstrong AA, Mahan AD, Luo J, Hammel M
RgGuinier 2.7 nm
Dmax 10.0 nm
VolumePorod 74 nm3

SASDDB5 – ...SANS, 100% D2O)

Lipid A export ATP-binding/permease protein MsbAMembrane scaffold protein 1D1 (deuterated, 75%)1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) experimental SAS data
SASREF CV model
Sample: Lipid A export ATP-binding/permease protein MsbA dimer, 133 kDa Escherichia coli protein
Membrane scaffold protein 1D1 (deuterated, 75%) dimer, 49 kDa protein
1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) , 1 kDa Escherichia coli
Buffer: 30 mM Tris, 150 mM NaCl, pH: 7.5
Experiment: SANS data collected at D11, ILL on 2017 Mar 9
Conformational States of ABC Transporter MsbA in a Lipid Environment Investigated by Small-Angle Scattering Using Stealth Carrier Nanodiscs. Structure 26(8):1072-1079.e4 (2018)
Josts I, Nitsche J, Maric S, Mertens HD, Moulin M, Haertlein M, Prevost S, Svergun DI, Busch S, Forsyth VT, Tidow H
RgGuinier 4.0 nm
Dmax 13.0 nm
VolumePorod 189 nm3

SASDDC5 – ...SANS, 100% D2O) + 1 mM ADP

Lipid A export ATP-binding/permease protein MsbAMembrane scaffold protein 1D1 (deuterated, 75%)1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) experimental SAS data
Lipid A export ATP-binding/permease protein MsbA Membrane scaffold protein 1D1 (deuterated, 75%) 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) Kratky plot
Sample: Lipid A export ATP-binding/permease protein MsbA dimer, 133 kDa Escherichia coli protein
Membrane scaffold protein 1D1 (deuterated, 75%) dimer, 49 kDa protein
1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) , 1 kDa Escherichia coli
Buffer: 30 mM Tris, 150 mM NaCl, 1 mM ADP, pH: 7.5
Experiment: SANS data collected at D11, ILL on 2017 Mar 9
Conformational States of ABC Transporter MsbA in a Lipid Environment Investigated by Small-Angle Scattering Using Stealth Carrier Nanodiscs. Structure 26(8):1072-1079.e4 (2018)
Josts I, Nitsche J, Maric S, Mertens HD, Moulin M, Haertlein M, Prevost S, Svergun DI, Busch S, Forsyth VT, Tidow H
RgGuinier 3.9 nm
Dmax 12.5 nm
VolumePorod 173 nm3

SASDNG5 – ...SANS

Neur_chan_LBD domain-containing protein experimental SAS data
GROMACS model
Sample: Neur_chan_LBD domain-containing protein pentamer, 342 kDa Desulfofustis sp. PB-SRB1 protein
Buffer: 20 mM Tris, 150 mM NaCl, 10 mM CaCl2, 0.5 mM deuterated n-Dodecyl-B-D-Maltoside, in D2O, pH: 7.5
Experiment: SANS data collected at D22, ILL on 2020 Aug 23
Biophysical characterization of calcium-binding and modulatory-domain dynamics in a pentameric ligand-gated ion channel
Marie Lycksell
RgGuinier 5.2 nm
Dmax 16.8 nm
VolumePorod 530 nm3

SASDNH5 – ...SANS

Neur_chan_LBD domain-containing protein experimental SAS data
Neur_chan_LBD domain-containing protein Kratky plot
Sample: Neur_chan_LBD domain-containing protein pentamer, 342 kDa Desulfofustis sp. PB-SRB1 protein
Buffer: 20 mM Tris, 150 mM NaCl, 10 mM EDTA, 0.5 mM deuterated n-Dodecyl-B-D-Maltoside, in D2O, pH: 7.5
Experiment: SANS data collected at D22, ILL on 2020 Aug 23
Biophysical characterization of calcium-binding and modulatory-domain dynamics in a pentameric ligand-gated ion channel
Marie Lycksell
RgGuinier 5.2 nm
Dmax 16.7 nm
VolumePorod 540 nm3

SASDFM5 – Mutant 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase, H110A tetramer, at pH 8.5

2-amino-3-carboxymuconate 6-semialdehyde decarboxylase experimental SAS data
CORAL model
Sample: 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase tetramer, 159 kDa Pseudomonas fluorescens protein
Buffer: 50 mM Tris, 5 mM DTT, pH: 8.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2018 Jul 15
Quaternary structure of α-amino-β-carboxymuconate-ϵ-semialdehyde decarboxylase (ACMSD) controls its activity. J Biol Chem 294(30):11609-11621 (2019)
Yang Y, Davis I, Matsui T, Rubalcava I, Liu A
RgGuinier 5.2 nm
Dmax 19.0 nm
VolumePorod 238 nm3

SASDFN5 – Wild type 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase, ACMSD tetramer, at pH 7.0

2-amino-3-carboxymuconate 6-semialdehyde decarboxylase experimental SAS data
CORAL model
Sample: 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase tetramer, 159 kDa Pseudomonas fluorescens protein
Buffer: 25 mM HEPES, 5 mM DTT, pH: 7
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2018 Jan 10
Quaternary structure of α-amino-β-carboxymuconate-ϵ-semialdehyde decarboxylase (ACMSD) controls its activity. J Biol Chem 294(30):11609-11621 (2019)
Yang Y, Davis I, Matsui T, Rubalcava I, Liu A
RgGuinier 4.7 nm
Dmax 17.5 nm
VolumePorod 195 nm3

SASDDY5 – AMPA subtype ionotropic Glutamate receptor GluA2 in the resting state (apo), in stealth DDM detergents

Glutamate receptor 2 experimental SAS data
Sample: Glutamate receptor 2 monomer, 368 kDa Rattus norvegicus protein
Buffer: D2O based buffer. 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O), pH: 7.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Sep 19
Small-angle neutron scattering studies on the AMPA receptor GluA2 in the resting, AMPA-bound and GYKI-53655-bound states. IUCrJ 5(Pt 6):780-793 (2018)
Larsen AH, Dorosz J, Thorsen TS, Johansen NT, Darwish T, Midtgaard SR, Arleth L, Kastrup JS
RgGuinier 6.0 nm
Dmax 17.9 nm
VolumePorod 396 nm3

SASDDZ5 – AMPA subtype ionotropic Glutamate receptor GluA2 in the AMPA bound state, in stealth DDM detergents, pH 7.5

Glutamate receptor 2 experimental SAS data
Sample: Glutamate receptor 2 monomer, 368 kDa Rattus norvegicus protein
Buffer: D2O based buffer. 1 mM AMPA, 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O), pH: 7.5
Experiment: SANS data collected at KWS1, FRM2 on 2016 Oct 19
Small-angle neutron scattering studies on the AMPA receptor GluA2 in the resting, AMPA-bound and GYKI-53655-bound states. IUCrJ 5(Pt 6):780-793 (2018)
Larsen AH, Dorosz J, Thorsen TS, Johansen NT, Darwish T, Midtgaard SR, Arleth L, Kastrup JS
RgGuinier 6.3 nm
Dmax 18.4 nm
VolumePorod 407 nm3

SASDD26 – AMPA subtype ionotropic Glutamate receptor GluA2 in the AMPA bound state, in stealth DDM detergents, pH 5.5

Glutamate receptor 2 experimental SAS data
Sample: Glutamate receptor 2 monomer, 368 kDa Rattus norvegicus protein
Buffer: D2O based buffer. 10 mM AMPA, 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O), pH: 5.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Sep 19
Small-angle neutron scattering studies on the AMPA receptor GluA2 in the resting, AMPA-bound and GYKI-53655-bound states. IUCrJ 5(Pt 6):780-793 (2018)
Larsen AH, Dorosz J, Thorsen TS, Johansen NT, Darwish T, Midtgaard SR, Arleth L, Kastrup JS
RgGuinier 6.5 nm
Dmax 18.9 nm
VolumePorod 899 nm3

SASDD36 – AMPA subtype ionotropic Glutamate receptor GluA2 in the GYKI-53655 bound state, in stealth DDM detergents

Glutamate receptor 2 experimental SAS data
Sample: Glutamate receptor 2 monomer, 368 kDa Rattus norvegicus protein
Buffer: D2O based buffer. 1 mM GYKI-53655, 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O), pH: 7.5
Experiment: SANS data collected at KWS1, FRM2 on 2016 Oct 19
Small-angle neutron scattering studies on the AMPA receptor GluA2 in the resting, AMPA-bound and GYKI-53655-bound states. IUCrJ 5(Pt 6):780-793 (2018)
Larsen AH, Dorosz J, Thorsen TS, Johansen NT, Darwish T, Midtgaard SR, Arleth L, Kastrup JS
RgGuinier 6.3 nm
Dmax 18.6 nm
VolumePorod 384 nm3

SASDKH6 – Sulfite reductase flavoprotein-43/hemoprotein heterodimer

Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein)Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) experimental SAS data
Sample: Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) monomer, 64 kDa Escherichia coli (strain … protein
Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) monomer, 42 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at ...SANS (BL-6), Spallation Neutron Source on 2018 Jul 11
Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase Journal of Structural Biology 213(2):107724 (2021)
Murray D, Weiss K, Stanley C, Nagy G, Stroupe M
RgGuinier 3.2 nm
Dmax 9.9 nm

SASDKJ6 – Sulfite reductase flavoprotein-60/hemoprotein heterodimer

Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein)Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) experimental SAS data
Sample: Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) monomer, 64 kDa Escherichia coli (strain … protein
Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) monomer, 61 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at ...SANS (BL-6), Spallation Neutron Source on 2018 Jul 11
Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase Journal of Structural Biology 213(2):107724 (2021)
Murray D, Weiss K, Stanley C, Nagy G, Stroupe M
RgGuinier 3.7 nm
Dmax 13.4 nm

SASDKK6 – Deuterated sulfite reductase hemoprotein

Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) experimental SAS data
Sample: Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) monomer, 64 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at ...SANS (BL-6), Spallation Neutron Source on 2020 May 28
Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase Journal of Structural Biology 213(2):107724 (2021)
Murray D, Weiss K, Stanley C, Nagy G, Stroupe M
RgGuinier 2.6 nm
Dmax 7.5 nm

SASDKL6 – Sulfite reductase flavoprotein-60 reduced with 10 molar equivalents sodium dithionite

Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) experimental SAS data
Sample: Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) monomer, 61 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at ...SANS (BL-6), Spallation Neutron Source on 2018 Jul 11
Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase Journal of Structural Biology 213(2):107724 (2021)
Murray D, Weiss K, Stanley C, Nagy G, Stroupe M
RgGuinier 3.4 nm
Dmax 12.2 nm

SASDKM6 – Sulfite reductase flavoprotein-60 (contrast-matched)/deuterated-hemoprotein heterodimer

Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) experimental SAS data
Sample: Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) monomer, 64 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at ...SANS (BL-6), Spallation Neutron Source on 2020 Jun 28
Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase Journal of Structural Biology 213(2):107724 (2021)
Murray D, Weiss K, Stanley C, Nagy G, Stroupe M
RgGuinier 2.4 nm
Dmax 6.6 nm

SASDKN6 – Sulfite reductase flavoprotein-60/deuterated-hemoprotein (contrast-matched) heterodimer

Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) experimental SAS data
Sample: Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) monomer, 61 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at ...SANS (BL-6), Spallation Neutron Source on 2020 Jun 26
Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase Journal of Structural Biology 213(2):107724 (2021)
Murray D, Weiss K, Stanley C, Nagy G, Stroupe M
RgGuinier 3.2 nm
Dmax 12.4 nm

SASDFV6 – DNA-binding protein HU-alpha, E38K/V42L double mutant

DNA-binding protein HU-alpha, E38K/V42L double mutant experimental SAS data
CHIMERA model
Sample: DNA-binding protein HU-alpha, E38K/V42L double mutant decamer, 95 kDa Escherichia coli protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, 1 mM PMSF, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Apr 23
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling (supplementary)
Soumya G Remesh
RgGuinier 3.0 nm
Dmax 10.5 nm
VolumePorod 53 nm3

SASDFW6 – DNA-binding protein HU-alpha, E38K/V42L double mutant bound to 80 bp DNA (ratio DNA:Protein 1:2)

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha, E38K/V42L double mutant experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha, E38K/V42L double mutant tetramer, 38 kDa Escherichia coli protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, 1 mM PMSF, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Apr 23
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling (supplementary)
Soumya G Remesh
RgGuinier 5.7 nm
Dmax 31.3 nm
VolumePorod 297 nm3

SASDFX6 – DNA-binding protein HU-alpha, E38K/V42L double mutant bound to 80 bp DNA (ratio DNA:Protein 1:4)

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha, E38K/V42L double mutant experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha, E38K/V42L double mutant tetramer, 38 kDa Escherichia coli protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, 1 mM PMSF, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Apr 23
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling (supplementary)
Soumya G Remesh
RgGuinier 5.7 nm
Dmax 25.7 nm
VolumePorod 195 nm3

SASDFY6 – DNA-binding protein HU-alpha, E38K/V42L double mutant bound to 80 bp DNA (ratio DNA:Protein 1:8)

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha, E38K/V42L double mutant experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha, E38K/V42L double mutant octamer, 76 kDa Escherichia coli protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, 1 mM PMSF, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Apr 23
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling (supplementary)
Soumya G Remesh
RgGuinier 5.8 nm
Dmax 28.1 nm
VolumePorod 296 nm3

SASDFZ6 – DNA-binding protein HU-alpha, E38K/V42L double mutant bound to 80 bp DNA (ratio DNA:Protein 1:16)

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha, E38K/V42L double mutant experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha, E38K/V42L double mutant 16-mer, 153 kDa Linked to wild-type … protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, 1 mM PMSF, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Apr 23
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling (supplementary)
Soumya G Remesh
RgGuinier 6.3 nm
Dmax 27.3 nm
VolumePorod 401 nm3

SASDK37SANS data for the sensory rhodopsin II / transducer complex in detergent at 0.15 M NaCl

Sensory rhodopsin II from Natronbacterium pharaonisSensory rhodopsin II transducer from Natronomonas pharaonis experimental SAS data
MEMPROT model
Sample: Sensory rhodopsin II from Natronbacterium pharaonis dimer, 53 kDa Natronomonas pharaonis protein
Sensory rhodopsin II transducer from Natronomonas pharaonis dimer, 116 kDa Natronomonas pharaonis protein
Buffer: 150 mM NaCl, 25 mM Na/Na-Pi, 1.0 mM EDTA, 0.05% DDM (D2O buffer), pH: 8
Experiment: SANS data collected at YuMO, IBR-2, FLNP, JINR on 2019 Jan 25
Molecular model of a sensor of two-component signaling system Scientific Reports 11(1) (2021)
Ryzhykau Y, Orekhov P, Rulev M, Vlasov A, Melnikov I, Volkov D, Nikolaev M, Zabelskii D, Murugova T, Chupin V, Rogachev A, Gruzinov A, Svergun D, Brennich M, Gushchin I, Soler-Lopez M, Bothe A, Büldt ...
RgGuinier 7.1 nm
Dmax 35.0 nm

SASDK47SANS data for the sensory rhodopsin II / transducer complex in detergent at 1.4 M NaCl

Sensory rhodopsin II from Natronbacterium pharaonisSensory rhodopsin II transducer from Natronomonas pharaonis experimental SAS data
MEMPROT model
Sample: Sensory rhodopsin II from Natronbacterium pharaonis dimer, 53 kDa Natronomonas pharaonis protein
Sensory rhodopsin II transducer from Natronomonas pharaonis dimer, 116 kDa Natronomonas pharaonis protein
Buffer: 1400 mM NaCl, 49.4 mM Na/Na-Pi, 1.0 mM EDTA, 0.05% DDM (D2O buffer), pH: 8
Experiment: SANS data collected at YuMO, IBR-2, FLNP, JINR on 2019 Feb 10
Molecular model of a sensor of two-component signaling system Scientific Reports 11(1) (2021)
Ryzhykau Y, Orekhov P, Rulev M, Vlasov A, Melnikov I, Volkov D, Nikolaev M, Zabelskii D, Murugova T, Chupin V, Rogachev A, Gruzinov A, Svergun D, Brennich M, Gushchin I, Soler-Lopez M, Bothe A, Büldt ...
RgGuinier 9.9 nm
Dmax 36.5 nm

SASDK57SANS data for the sensory rhodopsin II / transducer complex in detergent at 2.8 M NaCl

Sensory rhodopsin II from Natronbacterium pharaonisSensory rhodopsin II transducer from Natronomonas pharaonis experimental SAS data
MEMPROT model
Sample: Sensory rhodopsin II from Natronbacterium pharaonis dimer, 53 kDa Natronomonas pharaonis protein
Sensory rhodopsin II transducer from Natronomonas pharaonis dimer, 116 kDa Natronomonas pharaonis protein
Buffer: 2800 mM NaCl, 76.6 mM Na/Na-Pi, 1.0 mM EDTA, 0.05% DDM (D2O buffer), pH: 8
Experiment: SANS data collected at YuMO, IBR-2, FLNP, JINR on 2019 Feb 10
Molecular model of a sensor of two-component signaling system Scientific Reports 11(1) (2021)
Ryzhykau Y, Orekhov P, Rulev M, Vlasov A, Melnikov I, Volkov D, Nikolaev M, Zabelskii D, Murugova T, Chupin V, Rogachev A, Gruzinov A, Svergun D, Brennich M, Gushchin I, Soler-Lopez M, Bothe A, Büldt ...
RgGuinier 9.3 nm
Dmax 37.5 nm

SASDK67SANS data for the sensory rhodopsin II / transducer complex in detergent at 4.0 M NaCl

Sensory rhodopsin II from Natronbacterium pharaonisSensory rhodopsin II transducer from Natronomonas pharaonis experimental SAS data
MEMPROT model
Sample: Sensory rhodopsin II from Natronbacterium pharaonis dimer, 53 kDa Natronomonas pharaonis protein
Sensory rhodopsin II transducer from Natronomonas pharaonis dimer, 116 kDa Natronomonas pharaonis protein
Buffer: 4000 mM NaCl, 100 mM Na/Na-Pi, 1.0 mM EDTA, 0.05% DDM (D2O buffer), pH: 8
Experiment: SANS data collected at YuMO, IBR-2, FLNP, JINR on 2019 Jan 25
Molecular model of a sensor of two-component signaling system Scientific Reports 11(1) (2021)
Ryzhykau Y, Orekhov P, Rulev M, Vlasov A, Melnikov I, Volkov D, Nikolaev M, Zabelskii D, Murugova T, Chupin V, Rogachev A, Gruzinov A, Svergun D, Brennich M, Gushchin I, Soler-Lopez M, Bothe A, Büldt ...
RgGuinier 8.9 nm
Dmax 39.0 nm

SASDF87 – Mosqutio-larvicidal Binary (BinAB) toxin Receptor Cqm1 protein in 100% D2O

Binary toxin receptor Cqm1 protein experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Binary toxin receptor Cqm1 protein dimer, 129 kDa synthetic construct protein
Buffer: 25 mM HEPES, pH 7.5, 25 mM NaCl, in 100% D2O, pH: 7.5
Experiment: SANS data collected at SANS-I facility, Dhruva Reactor, Bhabha Atomic Research Centre on 2019 Apr 24
Small-angle neutron scattering studies suggest the mechanism of BinAB protein internalization IUCrJ 7(2) (2020)
Sharma M, Aswal V, Kumar V, Chidambaram R
RgGuinier 2.8 nm
Dmax 9.7 nm

SASDF97 – Complex of Binary toxin receptor (Cqm1) with deuterated BinB component protein in 100% D2O

Binary toxin receptor Cqm1 proteinDeuterated BinB component of mosquito-larvicidal Binary toxin experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Binary toxin receptor Cqm1 protein monomer, 65 kDa synthetic construct protein
Deuterated BinB component of mosquito-larvicidal Binary toxin monomer, 56 kDa synthetic construct protein
Buffer: 25 mM HEPES, pH 7.5, 25 mM NaCl, in 100% D2O, pH: 7.5
Experiment: SANS data collected at SANS-I facility, Dhruva Reactor, Bhabha Atomic Research Centre on 2019 Apr 23
Small-angle neutron scattering studies suggest the mechanism of BinAB protein internalization IUCrJ 7(2) (2020)
Sharma M, Aswal V, Kumar V, Chidambaram R
RgGuinier 1.9 nm
Dmax 7.3 nm

SASDFA7 – Receptor binding BinB protein of mosquito-larvicidal Binary toxin in 100% D2O

Lysinibacillus Mosquito-larvicidal receptor binding component experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Lysinibacillus Mosquito-larvicidal receptor binding component monomer, 53 kDa synthetic construct protein
Buffer: 25 mM HEPES, pH 7.5, 25 mM NaCl, in 100% D2O, pH: 7.5
Experiment: SANS data collected at SANS-I facility, Dhruva Reactor, Bhabha Atomic Research Centre on 2019 Apr 24
Small-angle neutron scattering studies suggest the mechanism of BinAB protein internalization IUCrJ 7(2) (2020)
Sharma M, Aswal V, Kumar V, Chidambaram R
RgGuinier 3.3 nm
Dmax 9.9 nm

SASDKM7 – Sulfite reductase flavoprotein-60

Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) experimental SAS data
Sample: Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) monomer, 61 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at ...SANS (BL-6), Spallation Neutron Source on 2018 Jul 11
NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation unique to this diflavin reductase Journal of Structural Biology 205(2):170-179 (2019)
Tavolieri A, Murray D, Askenasy I, Pennington J, McGarry L, Stanley C, Stroupe M
RgGuinier 3.2 nm
Dmax 11.6 nm
VolumePorod 60 nm3

SASDKN7 – Sulfite reductase flavoprotein-60-ΔAAPSQS

Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) experimental SAS data
Sample: Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) monomer, 61 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at ...SANS (BL-6), Spallation Neutron Source on 2018 Jul 11
NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation unique to this diflavin reductase Journal of Structural Biology 205(2):170-179 (2019)
Tavolieri A, Murray D, Askenasy I, Pennington J, McGarry L, Stanley C, Stroupe M
RgGuinier 3.2 nm
Dmax 11.3 nm
VolumePorod 73 nm3

SASDMJ8 – Sulfite reductase dodecamer

Sulfite reductase [NADPH] hemoprotein beta-componentSulfite reductase [NADPH] flavoprotein alpha-component (His-tagged) experimental SAS data
Sulfite reductase [NADPH] hemoprotein beta-component Sulfite reductase [NADPH] flavoprotein alpha-component (His-tagged) Kratky plot
Sample: Sulfite reductase [NADPH] hemoprotein beta-component tetramer, 256 kDa Escherichia coli (strain … protein
Sulfite reductase [NADPH] flavoprotein alpha-component (His-tagged) octamer, 565 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at ...SANS (BL-6), Spallation Neutron Source on 2021 Apr 3
Neutron scattering maps the higher-order assembly of NADPH-dependent assimilatory sulfite reductase. Biophys J (2022)
Murray DT, Walia N, Weiss KL, Stanley CB, Randolph PS, Nagy G, Stroupe ME
RgGuinier 11.0 nm
Dmax 32.5 nm
VolumePorod 1720 nm3

SASDMK8 – Sulfite reductase flavoprotein octamer

Sulfite reductase [NADPH] flavoprotein alpha-component (His-tagged) experimental SAS data
Sulfite reductase [NADPH] flavoprotein alpha-component (His-tagged) Kratky plot
Sample: Sulfite reductase [NADPH] flavoprotein alpha-component (His-tagged) octamer, 565 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at ...SANS (BL-6), Spallation Neutron Source on 2021 Apr 3
Neutron scattering maps the higher-order assembly of NADPH-dependent assimilatory sulfite reductase. Biophys J (2022)
Murray DT, Walia N, Weiss KL, Stanley CB, Randolph PS, Nagy G, Stroupe ME
RgGuinier 8.6 nm
Dmax 26.0 nm
VolumePorod 830 nm3

SASDML8 – Sulfite reductase hemoprotein

Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) experimental SAS data
Sample: Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) monomer, 64 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at ...SANS (BL-6), Spallation Neutron Source on 2018 Jul 13
Neutron scattering maps the higher-order assembly of NADPH-dependent assimilatory sulfite reductase. Biophys J (2022)
Murray DT, Walia N, Weiss KL, Stanley CB, Randolph PS, Nagy G, Stroupe ME
RgGuinier 2.3 nm
Dmax 7.2 nm
VolumePorod 71 nm3

SASDMM8 – Reconstituted sulfite reductase dodecamer with partially deuterated hemoprotein in 0% D2O

Sulfite reductase [NADPH] hemoprotein beta-componentSulfite reductase [NADPH] flavoprotein alpha-component (His-tagged) experimental SAS data
Sample: Sulfite reductase [NADPH] hemoprotein beta-component tetramer, 256 kDa Escherichia coli (strain … protein
Sulfite reductase [NADPH] flavoprotein alpha-component (His-tagged) octamer, 565 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at ...SANS (BL-6), Spallation Neutron Source on 2021 Apr 3
Neutron scattering maps the higher-order assembly of NADPH-dependent assimilatory sulfite reductase. Biophys J (2022)
Murray DT, Walia N, Weiss KL, Stanley CB, Randolph PS, Nagy G, Stroupe ME
RgGuinier 11.2 nm
Dmax 30.5 nm

SASDMN8 – Reconstituted sulfite reductase dodecamer with partially deuterated hemoprotein in 20% D2O

Sulfite reductase [NADPH] hemoprotein beta-componentSulfite reductase [NADPH] flavoprotein alpha-component (His-tagged) experimental SAS data
Sulfite reductase [NADPH] hemoprotein beta-component Sulfite reductase [NADPH] flavoprotein alpha-component (His-tagged) Kratky plot
Sample: Sulfite reductase [NADPH] hemoprotein beta-component tetramer, 256 kDa Escherichia coli (strain … protein
Sulfite reductase [NADPH] flavoprotein alpha-component (His-tagged) octamer, 565 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at ...SANS (BL-6), Spallation Neutron Source on 2021 Apr 3
Neutron scattering maps the higher-order assembly of NADPH-dependent assimilatory sulfite reductase. Biophys J (2022)
Murray DT, Walia N, Weiss KL, Stanley CB, Randolph PS, Nagy G, Stroupe ME
RgGuinier 11.3 nm
Dmax 29.5 nm

SASDMP8 – Reconstituted sulfite reductase dodecamer with partially deuterated hemoprotein in 41% D2O

Sulfite reductase [NADPH] hemoprotein beta-componentSulfite reductase [NADPH] flavoprotein alpha-component (His-tagged) experimental SAS data
Sample: Sulfite reductase [NADPH] hemoprotein beta-component tetramer, 256 kDa Escherichia coli (strain … protein
Sulfite reductase [NADPH] flavoprotein alpha-component (His-tagged) octamer, 565 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at ...SANS (BL-6), Spallation Neutron Source on 2021 Apr 3
Neutron scattering maps the higher-order assembly of NADPH-dependent assimilatory sulfite reductase. Biophys J (2022)
Murray DT, Walia N, Weiss KL, Stanley CB, Randolph PS, Nagy G, Stroupe ME
RgGuinier 11.4 nm
Dmax 28.5 nm
VolumePorod 417 nm3

SASDMQ8 – Reconstituted sulfite reductase dodecamer with partially deuterated hemoprotein in 86% D2O

Sulfite reductase [NADPH] hemoprotein beta-componentSulfite reductase [NADPH] flavoprotein alpha-component (His-tagged) experimental SAS data
Sample: Sulfite reductase [NADPH] hemoprotein beta-component tetramer, 256 kDa Escherichia coli (strain … protein
Sulfite reductase [NADPH] flavoprotein alpha-component (His-tagged) octamer, 565 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at ...SANS (BL-6), Spallation Neutron Source on 2021 Apr 3
Neutron scattering maps the higher-order assembly of NADPH-dependent assimilatory sulfite reductase. Biophys J (2022)
Murray DT, Walia N, Weiss KL, Stanley CB, Randolph PS, Nagy G, Stroupe ME
RgGuinier 6.8 nm
Dmax 22.0 nm
VolumePorod 460 nm3

SASDMR8 – Reconstituted sulfite reductase dodecamer with partially deuterated hemoprotein in 100% D2O

Sulfite reductase [NADPH] hemoprotein beta-componentSulfite reductase [NADPH] flavoprotein alpha-component (His-tagged) experimental SAS data
Sulfite reductase [NADPH] hemoprotein beta-component Sulfite reductase [NADPH] flavoprotein alpha-component (His-tagged) Kratky plot
Sample: Sulfite reductase [NADPH] hemoprotein beta-component tetramer, 256 kDa Escherichia coli (strain … protein
Sulfite reductase [NADPH] flavoprotein alpha-component (His-tagged) octamer, 565 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at ...SANS (BL-6), Spallation Neutron Source on 2021 Apr 3
Neutron scattering maps the higher-order assembly of NADPH-dependent assimilatory sulfite reductase. Biophys J (2022)
Murray DT, Walia N, Weiss KL, Stanley CB, Randolph PS, Nagy G, Stroupe ME
RgGuinier 8.5 nm
Dmax 25.1 nm

SASDMS8 – Sulfite reductase flavoprotein-60/deuterated-hemoprotein heterodimer in 0% D2O

Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein)Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) experimental SAS data
Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) Kratky plot
Sample: Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) monomer, 64 kDa Escherichia coli (strain … protein
Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) monomer, 61 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at ...SANS (BL-6), Spallation Neutron Source on 2021 Apr 3
Neutron scattering maps the higher-order assembly of NADPH-dependent assimilatory sulfite reductase. Biophys J (2022)
Murray DT, Walia N, Weiss KL, Stanley CB, Randolph PS, Nagy G, Stroupe ME
RgGuinier 3.4 nm
Dmax 13.0 nm

SASDMT8 – Sulfite reductase flavoprotein-60/deuterated-hemoprotein heterodimer in 41% D2O

Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein)Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) experimental SAS data
Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) Kratky plot
Sample: Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) monomer, 64 kDa Escherichia coli (strain … protein
Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) monomer, 61 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at ...SANS (BL-6), Spallation Neutron Source on 2021 Apr 3
Neutron scattering maps the higher-order assembly of NADPH-dependent assimilatory sulfite reductase. Biophys J (2022)
Murray DT, Walia N, Weiss KL, Stanley CB, Randolph PS, Nagy G, Stroupe ME
RgGuinier 2.2 nm
Dmax 6.6 nm

SASDHU8SANS study of the complex between mosquito-larvicidal BinB protein and the mosquito-larvicidal binary toxin receptor (Cqm1)

Binary larvicide subunit BinBSynthetic construct (mutant, His-tagged): Mosquito-larvicidal BinAB toxin receptor protein (Neutral and basic amino acid transport protein rBAT) experimental SAS data
OTHER model
Sample: Binary larvicide subunit BinB monomer, 53 kDa Lysinibacillus sphaericus protein
Synthetic construct (mutant, His-tagged): Mosquito-larvicidal BinAB toxin receptor protein (Neutral and basic amino acid transport protein rBAT) monomer, 65 kDa Culex quinquefasciatus protein
Buffer: 25 mM HEPES, pH 7.5, 25 mM NaCl, in 100% D2O, pH: 7.5
Experiment: SANS data collected at SANS-I facility, Dhruva Reactor, Bhabha Atomic Research Centre on 2019 Apr 26
Liposome-Based Study Provides Insight into Cellular Internalization Mechanism of Mosquito-Larvicidal BinAB Toxin. J Membr Biol (2020)
Sharma M, Kumar A, Kumar V
RgGuinier 3.7 nm
Dmax 12.9 nm
VolumePorod 174 nm3

SASDMU8 – Sulfite reductase flavoprotein-60/deuterated-hemoprotein heterodimer in 86% D2O

Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein)Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) experimental SAS data
Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) Kratky plot
Sample: Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) monomer, 64 kDa Escherichia coli (strain … protein
Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) monomer, 61 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at ...SANS (BL-6), Spallation Neutron Source on 2021 Apr 3
Neutron scattering maps the higher-order assembly of NADPH-dependent assimilatory sulfite reductase. Biophys J (2022)
Murray DT, Walia N, Weiss KL, Stanley CB, Randolph PS, Nagy G, Stroupe ME
RgGuinier 3.1 nm
Dmax 12.4 nm

SASDMV8 – Sulfite reductase flavoprotein-60/deuterated-hemoprotein heterodimer in 100% D2O

Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein)Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) experimental SAS data
Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) Kratky plot
Sample: Sulfite reductase [NADPH] hemoprotein beta-component (Assimilatory NADPH-dependent sulfite reductase hemoprotein) monomer, 64 kDa Escherichia coli (strain … protein
Sulfite reductase [NADPH] flavoprotein alpha-component (Assimilatory NADPH-dependent sulfite reductase flavoprotein) monomer, 61 kDa Escherichia coli (strain … protein
Buffer: 50 mM KPi, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at ...SANS (BL-6), Spallation Neutron Source on 2021 Apr 3
Neutron scattering maps the higher-order assembly of NADPH-dependent assimilatory sulfite reductase. Biophys J (2022)
Murray DT, Walia N, Weiss KL, Stanley CB, Randolph PS, Nagy G, Stroupe ME
RgGuinier 4.0 nm
Dmax 13.9 nm

SASDJ79 – ...SANS

Sensory rhodopsin II from Natronbacterium pharaonisSensory rhodopsin II transducer from Natronomonas pharaonis experimental SAS data
MEMPROT model
Sample: Sensory rhodopsin II from Natronbacterium pharaonis dimer, 53 kDa Natronomonas pharaonis protein
Sensory rhodopsin II transducer from Natronomonas pharaonis dimer, 116 kDa Natronomonas pharaonis protein
Buffer: 150 mM NaCl, 25 mM Na/Na-Pi, 1.0 mM EDTA, 0.05% DDM (D2O buffer), pH: 8
Experiment: SANS data collected at YuMO, IBR-2, FLNP, JINR on 2019 Jan 25
Ambiguities in and completeness of SAS data analysis of membrane proteins: the case of the sensory rhodopsin II–transducer complex Acta Crystallographica Section D Structural Biology 77(11) (2021)
Ryzhykau Y, Vlasov A, Orekhov P, Rulev M, Rogachev A, Vlasova A, Kazantsev A, Verteletskiy D, Skoi V, Brennich M, Pernot P, Murugova T, Gordeliy V, Kuklin A
RgGuinier 8.9 nm
Dmax 39.0 nm

SASDJ89 – ...SANS

Sensory rhodopsin II from Natronbacterium pharaonisSensory rhodopsin II transducer from Natronomonas pharaonis experimental SAS data
GASBOR model
Sample: Sensory rhodopsin II from Natronbacterium pharaonis dimer, 53 kDa Natronomonas pharaonis protein
Sensory rhodopsin II transducer from Natronomonas pharaonis dimer, 116 kDa Natronomonas pharaonis protein
Buffer: 1400 mM NaCl, 49.4 mM Na/Na-Pi, 1.0 mM EDTA, 0.05% DDM (D2O buffer), pH: 8
Experiment: SANS data collected at YuMO, IBR-2, FLNP, JINR on 2019 Feb 10
Ambiguities in and completeness of SAS data analysis of membrane proteins: the case of the sensory rhodopsin II–transducer complex Acta Crystallographica Section D Structural Biology 77(11) (2021)
Ryzhykau Y, Vlasov A, Orekhov P, Rulev M, Rogachev A, Vlasova A, Kazantsev A, Verteletskiy D, Skoi V, Brennich M, Pernot P, Murugova T, Gordeliy V, Kuklin A
RgGuinier 8.6 nm
Dmax 39.0 nm

SASDC99 – ...SANS

Apolipoprotein A-I1,2-dimyristoyl-sn-glycero-3-phosphocholine experimental SAS data
Apolipoprotein A-I 1,2-dimyristoyl-sn-glycero-3-phosphocholine Kratky plot
Sample: Apolipoprotein A-I dimer, 50 kDa Mus musculus protein
1,2-dimyristoyl-sn-glycero-3-phosphocholine , 92 kDa
Buffer: PBS in D2O, pH: 7.4
Experiment: SANS data collected at NG7, NIST Center for Neutron Research on 2015 Nov 25
Small-angle X-ray and neutron scattering demonstrates that cell-free expression produces properly formed disc-shaped nanolipoprotein particles. Protein Sci 27(3):780-789 (2018)
Cleveland TE 4th, He W, Evans AC, Fischer NO, Lau EY, Coleman MA, Butler P
RgGuinier 3.1 nm
Dmax 9.1 nm

SASDJ99 – ...SANS

Sensory rhodopsin II from Natronbacterium pharaonisSensory rhodopsin II transducer from Natronomonas pharaonis experimental SAS data
GASBOR model
Sample: Sensory rhodopsin II from Natronbacterium pharaonis dimer, 53 kDa Natronomonas pharaonis protein
Sensory rhodopsin II transducer from Natronomonas pharaonis dimer, 116 kDa Natronomonas pharaonis protein
Buffer: 2800 mM NaCl, 76.6 mM Na/Na-Pi, 1.0 mM EDTA, 0.05% DDM (D2O buffer), pH: 8
Experiment: SANS data collected at YuMO, IBR-2, FLNP, JINR on 2019 Feb 10
Ambiguities in and completeness of SAS data analysis of membrane proteins: the case of the sensory rhodopsin II–transducer complex Acta Crystallographica Section D Structural Biology 77(11) (2021)
Ryzhykau Y, Vlasov A, Orekhov P, Rulev M, Rogachev A, Vlasova A, Kazantsev A, Verteletskiy D, Skoi V, Brennich M, Pernot P, Murugova T, Gordeliy V, Kuklin A
RgGuinier 9.0 nm
Dmax 39.0 nm

SASDJA9 – ...SANS

Sensory rhodopsin II from Natronbacterium pharaonisSensory rhodopsin II transducer from Natronomonas pharaonis experimental SAS data
GASBOR model
Sample: Sensory rhodopsin II from Natronbacterium pharaonis dimer, 53 kDa Natronomonas pharaonis protein
Sensory rhodopsin II transducer from Natronomonas pharaonis dimer, 116 kDa Natronomonas pharaonis protein
Buffer: 4000 mM NaCl, 100 mM Na/Na-Pi, 1.0 mM EDTA, 0.05% DDM (D2O buffer), pH: 8
Experiment: SANS data collected at YuMO, IBR-2, FLNP, JINR on 2019 Jan 25
Ambiguities in and completeness of SAS data analysis of membrane proteins: the case of the sensory rhodopsin II–transducer complex Acta Crystallographica Section D Structural Biology 77(11) (2021)
Ryzhykau Y, Vlasov A, Orekhov P, Rulev M, Rogachev A, Vlasova A, Kazantsev A, Verteletskiy D, Skoi V, Brennich M, Pernot P, Murugova T, Gordeliy V, Kuklin A
RgGuinier 10.4 nm
Dmax 39.0 nm

SASDCB9 – ...SANS

Apolipoprotein A-I1,2-dimyristoyl-d54-sn-glycero-3-phosphocholine experimental SAS data
Apolipoprotein A-I 1,2-dimyristoyl-d54-sn-glycero-3-phosphocholine Kratky plot
Sample: Apolipoprotein A-I dimer, 50 kDa Mus musculus protein
1,2-dimyristoyl-d54-sn-glycero-3-phosphocholine , 99 kDa
Buffer: PBS in D2O, pH: 7.4
Experiment: SANS data collected at NG7, NIST Center for Neutron Research on 2016 Apr 11
Small-angle X-ray and neutron scattering demonstrates that cell-free expression produces properly formed disc-shaped nanolipoprotein particles. Protein Sci 27(3):780-789 (2018)
Cleveland TE 4th, He W, Evans AC, Fischer NO, Lau EY, Coleman MA, Butler P
RgGuinier 4.3 nm
Dmax 10.7 nm

SASDCC9 – ...SANS

Apolipoprotein A-I1,2-dimyristoyl-sn-glycero-3-phosphocholine experimental SAS data
Apolipoprotein A-I 1,2-dimyristoyl-sn-glycero-3-phosphocholine Kratky plot
Sample: Apolipoprotein A-I dimer, 50 kDa Mus musculus protein
1,2-dimyristoyl-sn-glycero-3-phosphocholine , 92 kDa
Buffer: PBS in 42% D2O, pH: 7.4
Experiment: SANS data collected at NGB30, NIST Center for Neutron Research on 2015 Dec 11
Small-angle X-ray and neutron scattering demonstrates that cell-free expression produces properly formed disc-shaped nanolipoprotein particles. Protein Sci 27(3):780-789 (2018)
Cleveland TE 4th, He W, Evans AC, Fischer NO, Lau EY, Coleman MA, Butler P
RgGuinier 2.9 nm
Dmax 7.3 nm

SASDCF9 – ...SANS

1,2-dimyristoyl-sn-glycero-3-phosphocholineApolipoprotein A-I experimental SAS data
1,2-dimyristoyl-sn-glycero-3-phosphocholine Apolipoprotein A-I Kratky plot
Sample: 1,2-dimyristoyl-sn-glycero-3-phosphocholine , 92 kDa
Apolipoprotein A-I dimer, 52 kDa Mus musculus protein
Buffer: PBS in D2O, pH: 7.4
Experiment: SANS data collected at NG7, NIST Center for Neutron Research on 2015 Nov 25
Small-angle X-ray and neutron scattering demonstrates that cell-free expression produces properly formed disc-shaped nanolipoprotein particles. Protein Sci 27(3):780-789 (2018)
Cleveland TE 4th, He W, Evans AC, Fischer NO, Lau EY, Coleman MA, Butler P
RgGuinier 3.5 nm
Dmax 12.5 nm

SASDCG9 – ...SANS

1,2-dimyristoyl-sn-glycero-3-phosphocholineApolipoprotein A-I experimental SAS data
1,2-dimyristoyl-sn-glycero-3-phosphocholine Apolipoprotein A-I Kratky plot
Sample: 1,2-dimyristoyl-sn-glycero-3-phosphocholine , 92 kDa
Apolipoprotein A-I dimer, 52 kDa Mus musculus protein
Buffer: PBS in D2O, pH: 7.4
Experiment: SANS data collected at NG7, NIST Center for Neutron Research on 2015 Nov 25
Small-angle X-ray and neutron scattering demonstrates that cell-free expression produces properly formed disc-shaped nanolipoprotein particles. Protein Sci 27(3):780-789 (2018)
Cleveland TE 4th, He W, Evans AC, Fischer NO, Lau EY, Coleman MA, Butler P
RgGuinier 3.3 nm
Dmax 10.0 nm

SASDDJ9 – ...SANS)

R1-3 human dystrophin fragment experimental SAS data
YASARA model
Sample: R1-3 human dystrophin fragment monomer, 39 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% D2O, pD 7.5, pH: 7.1
Experiment: SANS data collected at D22, ILL on 2016 Nov 7
Human Dystrophin Structural Changes upon Binding to Anionic Membrane Lipids. Biophys J 115(7):1231-1239 (2018)
Dos Santos Morais R, Delalande O, Pérez J, Mias-Lucquin D, Lagarrigue M, Martel A, Molza AE, Chéron A, Raguénès-Nicol C, Chenuel T, Bondon A, Appavou MS, Le Rumeur E, Combet S, Hubert JF
RgGuinier 4.2 nm
Dmax 17.7 nm
VolumePorod 46 nm3

SASDDK9 – ...SANS)

R1-3 human dystrophin fragment experimental SAS data
DAMMIF model
Sample: R1-3 human dystrophin fragment monomer, 39 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% D2O, pD 7.5, pH: 7.1
Experiment: SANS data collected at D22, ILL on 2016 Nov 7
Human Dystrophin Structural Changes upon Binding to Anionic Membrane Lipids. Biophys J 115(7):1231-1239 (2018)
Dos Santos Morais R, Delalande O, Pérez J, Mias-Lucquin D, Lagarrigue M, Martel A, Molza AE, Chéron A, Raguénès-Nicol C, Chenuel T, Bondon A, Appavou MS, Le Rumeur E, Combet S, Hubert JF
RgGuinier 4.1 nm
Dmax 17.8 nm
VolumePorod 50 nm3

SASDDL9 – ...SANS)

R1-3 human dystrophin fragment experimental SAS data
YASARA model
Sample: R1-3 human dystrophin fragment monomer, 39 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% D2O, pD 7.5, pH: 7.1
Experiment: SANS data collected at D22, ILL on 2016 Nov 7
Human Dystrophin Structural Changes upon Binding to Anionic Membrane Lipids. Biophys J 115(7):1231-1239 (2018)
Dos Santos Morais R, Delalande O, Pérez J, Mias-Lucquin D, Lagarrigue M, Martel A, Molza AE, Chéron A, Raguénès-Nicol C, Chenuel T, Bondon A, Appavou MS, Le Rumeur E, Combet S, Hubert JF
RgGuinier 6.2 nm
Dmax 24.8 nm
VolumePorod 100 nm3

SASDFR6 – DNA-binding protein HU-alpha, E34K mutant bound to 80 bp DNA (ratio DNA:Protein 1:1)

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha, E34K experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha, E34K , 228 kDa Escherichia coli protein
Buffer: 20mM HEPES, 100mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Jul 8
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
Remesh SG, Verma SC, Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 6.1 nm
Dmax 21.9 nm
VolumePorod 251 nm3

SASDBV9 – Immunoglobulin domain 4 of Nucleoporin Pom152 (Pom152 Ig-4: amino acids 718-820)

Nucleoporin POM152 experimental SAS data
MODELLER model
Sample: Nucleoporin POM152 monomer, 12 kDa Saccharomyces cerevisiae protein
Buffer: 10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
Upla P, Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J
RgGuinier 1.8 nm
Dmax 6.7 nm
VolumePorod 18 nm3

SASDFS6 – DNA-binding protein HU-alpha, E34K mutant bound to 80 bp DNA (ratio DNA:Protein 1:2.5)

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha, E34K experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha, E34K , 267 kDa Escherichia coli protein
Buffer: 20mM HEPES, 100mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Jul 8
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
Remesh SG, Verma SC, Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 7.0 nm
Dmax 25.0 nm
VolumePorod 386 nm3

SASDBW9 – Immunoglobulin domains 4,5 of Nucleoporin Pom152 (Pom152 Ig-4,5: amino acids 718-920)

Nucleoporin POM152 experimental SAS data
DAMMIN model
Sample: Nucleoporin POM152 monomer, 24 kDa Saccharomyces cerevisiae protein
Buffer: 10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
Upla P, Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J
RgGuinier 2.7 nm
Dmax 9.4 nm
VolumePorod 23 nm3