Browse by DISSEMINATION: Published

SASDNU7 – Obscurin Ig domains 12/13 at neutral pH

Obscurin experimental SAS data
Obscurin Kratky plot
Sample: Obscurin monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM Tris, 50 mM NaCl, 0.35 mM NaN3, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2021 May 18
The N-terminus of obscurin is flexible in solution. Proteins (2022)
Mauriello GE, Moncure GE, Nowzari RA, Miller CJ, Wright NT
RgGuinier 2.8 nm
Dmax 10.5 nm
VolumePorod 28 nm3

SASDNV7 – Obscurin Ig domains 11/12 at neutral pH

Obscurin experimental SAS data
Obscurin Kratky plot
Sample: Obscurin monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM Tris, 50 mM NaCl, 0.35 mM NaN3, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Nov 18
The N-terminus of obscurin is flexible in solution. Proteins (2022)
Mauriello GE, Moncure GE, Nowzari RA, Miller CJ, Wright NT
RgGuinier 3.7 nm
Dmax 18.0 nm
VolumePorod 66 nm3

SASDNW7 – Obscurin Ig domains 12/13, short at neutral pH

Obscurin Ig domains 12/13 short experimental SAS data
MULTIFOXS model
Sample: Obscurin Ig domains 12/13 short monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM Tris, 50 mM NaCl, 0.35 mM NaN3, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2021 Oct 20
The N-terminus of obscurin is flexible in solution. Proteins (2022)
Mauriello GE, Moncure GE, Nowzari RA, Miller CJ, Wright NT
RgGuinier 2.5 nm
Dmax 9.0 nm
VolumePorod 25 nm3

SASDNX7 – Obscurin Ig domains 12/13, long at neutral pH

Obscurin Ig domains 12/13 long experimental SAS data
MULTIFOXS model
Sample: Obscurin Ig domains 12/13 long monomer, 22 kDa Homo sapiens protein
Buffer: 20 mM Tris, 50 mM NaCl, 0.35 mM NaN3, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2021 Oct 20
The N-terminus of obscurin is flexible in solution. Proteins (2022)
Mauriello GE, Moncure GE, Nowzari RA, Miller CJ, Wright NT
RgGuinier 2.9 nm
Dmax 10.0 nm
VolumePorod 26 nm3

SASDP34 – Ubiquitin-conjugating enzyme E2 conjugated to deuterated Ubiquitin (SANS data at 0% v/v D2O, plus additional SANS with contrast variation and SAXS datasets)

Ubiquitin-conjugating enzyme E2 D1 (S22R, C85K, D87S)Ubiquitin experimental SAS data
MONSA model
Sample: Ubiquitin-conjugating enzyme E2 D1 (S22R, C85K, D87S) monomer, 17 kDa Homo sapiens protein
Ubiquitin monomer, 9 kDa Homo sapiens protein
Buffer: 50 mM Tris, 150 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SANS data collected at Quokka - Small Angle Neutron Scattering, Australian Centre for Neutron Scattering (ANSTO) on 2019 May 24
Production and characterisation of modularly deuterated UBE2D1–Ub conjugate by small angle neutron and X-ray scattering European Biophysics Journal (2022)
Pietras Z, Duff A, Morad V, Wood K, Jeffries C, Sunnerhagen M
RgGuinier 2.1 nm
Dmax 7.4 nm

SASDQP5 – Phosphoprotein of Borna disease virus

Phosphoprotein experimental SAS data
Phosphoprotein of Borna disease virus Rg histogram
Sample: Phosphoprotein tetramer, 90 kDa Borna disease virus … protein
Buffer: 20 mM HEPES, 150 mM NaCl, 5 mM β- mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Sep 1
Borna Disease Virus 1 Phosphoprotein Forms a Tetramer and Interacts with Host Factors Involved in DNA Double-Strand Break Repair and mRNA Processing. Viruses 14(11) (2022)
Tarbouriech N, Chenavier F, Kawasaki J, Bachiri K, Bourhis JM, Legrand P, Freslon LL, Laurent EMN, Suberbielle E, Ruigrok RWH, Tomonaga K, Gonzalez-Dunia D, Horie M, Coyaud E, Crépin T
RgGuinier 6.1 nm
Dmax 21.5 nm
VolumePorod 225 nm3

SASDQQ5 – Oligomerisation domain of phosphoprotein from Borna disease virus

Phosphoprotein experimental SAS data
DAMMIF model
Sample: Phosphoprotein tetramer, 47 kDa Borna disease virus … protein
Buffer: 20 mM HEPES, 150 mM NaCl, 5 mM β- mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Sep 1
Borna Disease Virus 1 Phosphoprotein Forms a Tetramer and Interacts with Host Factors Involved in DNA Double-Strand Break Repair and mRNA Processing. Viruses 14(11) (2022)
Tarbouriech N, Chenavier F, Kawasaki J, Bachiri K, Bourhis JM, Legrand P, Freslon LL, Laurent EMN, Suberbielle E, Ruigrok RWH, Tomonaga K, Gonzalez-Dunia D, Horie M, Coyaud E, Crépin T
RgGuinier 4.5 nm
Dmax 17.0 nm
VolumePorod 66 nm3

SASDQR5 – Oligomerisation domain of phosphoprotein from Munia bornavirus

Phosphoprotein oligomerisation domain experimental SAS data
DAMMIF model
Sample: Phosphoprotein oligomerisation domain tetramer, 50 kDa protein
Buffer: 20 mM HEPES, 150 mM NaCl, 5 mM β- mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Sep 1
Borna Disease Virus 1 Phosphoprotein Forms a Tetramer and Interacts with Host Factors Involved in DNA Double-Strand Break Repair and mRNA Processing. Viruses 14(11) (2022)
Tarbouriech N, Chenavier F, Kawasaki J, Bachiri K, Bourhis JM, Legrand P, Freslon LL, Laurent EMN, Suberbielle E, Ruigrok RWH, Tomonaga K, Gonzalez-Dunia D, Horie M, Coyaud E, Crépin T
RgGuinier 4.6 nm
Dmax 17.8 nm
VolumePorod 70 nm3

SASDQS5 – Oligomerisation domain of phosphoprotein from Gaboon viper virus

Phosphoprotein experimental SAS data
DAMMIF model
Sample: Phosphoprotein tetramer, 52 kDa Gaboon viper virus … protein
Buffer: 20 mM HEPES, 150 mM NaCl, 5 mM β- mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Sep 1
Borna Disease Virus 1 Phosphoprotein Forms a Tetramer and Interacts with Host Factors Involved in DNA Double-Strand Break Repair and mRNA Processing. Viruses 14(11) (2022)
Tarbouriech N, Chenavier F, Kawasaki J, Bachiri K, Bourhis JM, Legrand P, Freslon LL, Laurent EMN, Suberbielle E, Ruigrok RWH, Tomonaga K, Gonzalez-Dunia D, Horie M, Coyaud E, Crépin T
RgGuinier 4.6 nm
Dmax 17.5 nm
VolumePorod 75 nm3

SASDNM5 – Skp-like protein, SKP

Skp-like protein experimental SAS data
Skp-like protein, SKP Rg histogram
Sample: Skp-like protein trimer, 55 kDa Pseudomonas aeruginosa (strain … protein
Buffer: 20 mM Tris, 100 mM NaCl, 10 % glycerol, pH: 8
Experiment: SAXS data collected at Xenocs Xeuss 2.0 Q-Xoom, Center for Structural Studies, Heinrich-Heine-University on 2021 Feb 26
The periplasmic chaperone Skp prevents misfolding of the secretory lipase A from Pseudomonas aeruginosa Frontiers in Molecular Biosciences 9 (2022)
Papadopoulos A, Busch M, Reiners J, Hachani E, Baeumers M, Berger J, Schmitt L, Jaeger K, Kovacic F, Smits S, Kedrov A
RgGuinier 3.5 nm
Dmax 11.1 nm
VolumePorod 172 nm3