Browse by MODEL: Ab initio only

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 EQ-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 EQ-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 EQ-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

SASDL62 – The truncated RTX domain of adenylate cyclase toxin CyaA - construct RTX-1 (amino acids 1132-1294 and 1562-1681 of CyaA)

hybrid RTX-1 construct (amino acids 1132-1294 and 1562-1681 of CyaA) experimental SAS data
DAMFILT model
Sample: Hybrid RTX-1 construct (amino acids 1132-1294 and 1562-1681 of CyaA) monomer, 30 kDa Bordetella pertussis protein
Buffer: 10 mM Tris HCl, 150 mM NaCl, 10 mM CaCl₂, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Dec 1
Almost half of the RTX domain is dispensable for complement receptor 3 binding and cell-invasive activity of the adenylate cyclase toxin. J Biol Chem :100833 (2021)
Espinosa-Vinals CA, Masin J, Holubova J, Stanek O, Jurnecka D, Osicka R, Sebo P, Bumba L
RgGuinier 2.4 nm
Dmax 8.2 nm
VolumePorod 41 nm3

SASDL72 – The truncated RTX domain of adenylate cyclase toxin CyaA - construct RTX-2 (amino acids 1132-1303 and 1562-1681 of CyaA)

hybrid RTX-2 construct (amino acids 1132-1303 and 1562-1681 of CyaA) experimental SAS data
DAMMIF model
Sample: Hybrid RTX-2 construct (amino acids 1132-1303 and 1562-1681 of CyaA) monomer, 31 kDa Bordetella pertussis protein
Buffer: 10 mM Tris HCl, 150 mM NaCl, 10 mM CaCl₂, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Dec 1
Almost half of the RTX domain is dispensable for complement receptor 3 binding and cell-invasive activity of the adenylate cyclase toxin. J Biol Chem :100833 (2021)
Espinosa-Vinals CA, Masin J, Holubova J, Stanek O, Jurnecka D, Osicka R, Sebo P, Bumba L
RgGuinier 2.3 nm
Dmax 8.0 nm
VolumePorod 37 nm3

SASDK58 – Histidine kinase AdeS - cytoplasmic domain

Histidine kinase experimental SAS data
OTHER model
Sample: Histidine kinase hexamer, 186 kDa Acinetobacter baumannii protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2019 Jun 19
Proteolysis and multimerization regulate signaling along the two-component regulatory system AdeRS. iScience 24(5):102476 (2021)
Ouyang Z, Zheng F, Zhu L, Felix J, Wu D, Wu K, Gutsche I, Wu Y, Hwang PM, She J, Wen Y
RgGuinier 4.6 nm
Dmax 16.3 nm
VolumePorod 378 nm3

SASDK24 – Signal recognition particle SRP9/14 heterodimer from Plasmodium falciparum

Signal recognition particle 9Signal recognition particle 14 experimental SAS data
DAMMIN model
Sample: Signal recognition particle 9 monomer, 12 kDa Plasmodium falciparum protein
Signal recognition particle 14 monomer, 12 kDa Plasmodium falciparum protein
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, 10 mM MgCl2, 10 mM KCl, 1mM DTT, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Feb 22
Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation. Commun Biol 4(1):600 (2021)
Soni K, Kempf G, Manalastas-Cantos K, Hendricks A, Flemming D, Guizetti J, Simon B, Frischknecht F, Svergun DI, Wild K, Sinning I
RgGuinier 2.1 nm
Dmax 7.2 nm
VolumePorod 47 nm3

SASDK34 – Full length SRP Alu RNA from Plasmodium falciparum

Full-length SRP Alu RNA experimental SAS data
DAMMIN model
Sample: Full-length SRP Alu RNA monomer, 38 kDa Plasmodium falciparum RNA
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, 10 mM MgCl2, 10 mM KCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Jun 22
Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation. Commun Biol 4(1):600 (2021)
Soni K, Kempf G, Manalastas-Cantos K, Hendricks A, Flemming D, Guizetti J, Simon B, Frischknecht F, Svergun DI, Wild K, Sinning I
RgGuinier 3.3 nm
Dmax 11.8 nm
VolumePorod 63 nm3

SASDK44 – The 5' domain of SRP Alu RNA from Plasmodium falciparum

SRP Alu RNA 5' domain experimental SAS data
DAMMIN model
Sample: SRP Alu RNA 5' domain monomer, 24 kDa Plasmodium falciparum RNA
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, 10 mM MgCl2, 10 mM KCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Jun 22
Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation. Commun Biol 4(1):600 (2021)
Soni K, Kempf G, Manalastas-Cantos K, Hendricks A, Flemming D, Guizetti J, Simon B, Frischknecht F, Svergun DI, Wild K, Sinning I
RgGuinier 3.3 nm
Dmax 11.5 nm
VolumePorod 38 nm3

SASDK54 – Signal recognition particle SRP9/14 heterodimer in complex with full length SRP Alu RNA from Plasmodium falciparum

Signal recognition particle 9Signal recognition particle 14Full-length SRP Alu RNA experimental SAS data
MONSA model
Sample: Signal recognition particle 9 monomer, 12 kDa Plasmodium falciparum protein
Signal recognition particle 14 monomer, 12 kDa Plasmodium falciparum protein
Full-length SRP Alu RNA monomer, 38 kDa Plasmodium falciparum RNA
Buffer: 20 mM HEPES pH 7.5, 150 mM NaCl, 10 mM MgCl2, 10 mM KCl, 1mM DTT, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Jun 22
Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation. Commun Biol 4(1):600 (2021)
Soni K, Kempf G, Manalastas-Cantos K, Hendricks A, Flemming D, Guizetti J, Simon B, Frischknecht F, Svergun DI, Wild K, Sinning I
RgGuinier 3.5 nm
Dmax 12.0 nm
VolumePorod 120 nm3