Search

  
Advanced search  

128 hits found for Martins

SASDE32 – Mothers against decapentaplegic homolog 5 - Smad5 MH1

Mothers against decapentaplegic homolog 5 experimental SAS data
Mothers against decapentaplegic homolog 5 Kratky plot
Sample: Mothers against decapentaplegic homolog 5 , 15 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2018 Feb 14
Unveiling the dimer/monomer propensities of Smad MH1-DNA complexes (2019)
Ruiz L, Kaczmarska Z, Gomes T, Aragón E, Torner C, Freier R, Bagiński B, Martin-Malpartida P, de Martin Garrido N, Márquez J, Cordeiro T, Pluta R, Macias M
RgGuinier 1.9 nm
Dmax 6.6 nm
VolumePorod 32 nm3

SASDE42 – Mothers against decapentaplegic homolog 8_9 - Smad8_9 MH1

Mothers against decapentaplegic homolog 8_9 experimental SAS data
Mothers against decapentaplegic homolog 8_9 Kratky plot
Sample: Mothers against decapentaplegic homolog 8_9 , 15 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2018 Mar 1
Unveiling the dimer/monomer propensities of Smad MH1-DNA complexes (2019)
Ruiz L, Kaczmarska Z, Gomes T, Aragón E, Torner C, Freier R, Bagiński B, Martin-Malpartida P, de Martin Garrido N, Márquez J, Cordeiro T, Pluta R, Macias M
RgGuinier 1.9 nm
Dmax 6.5 nm
VolumePorod 34 nm3

SASDLA2 – Mothers against decapentaplegic homolog 2, SMAD2 phosphomimetic mutant 0.5 mg/ml

Mothers against decapentaplegic homolog 2 (C-terminus phosphomimetic mutant) experimental SAS data
Mothers against decapentaplegic homolog 2 (C-terminus phosphomimetic mutant) Kratky plot
Sample: Mothers against decapentaplegic homolog 2 (C-terminus phosphomimetic mutant) , 53 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2016 Apr 4
Conformational landscape of multidomain SMAD proteins Computational and Structural Biotechnology Journal (2021)
Gomes T, Martin-Malpartida P, Ruiz L, Aragón E, Cordeiro T, Macias M
RgGuinier 5.1 nm
Dmax 20.0 nm

SASDLB2 – Mothers against decapentaplegic homolog 2, SMAD2 phosphomimetic mutant 1 mg/ml

Mothers against decapentaplegic homolog 2 (C-terminus phosphomimetic mutant) experimental SAS data
Mothers against decapentaplegic homolog 2 (C-terminus phosphomimetic mutant) Kratky plot
Sample: Mothers against decapentaplegic homolog 2 (C-terminus phosphomimetic mutant) , 53 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2016 Apr 4
Conformational landscape of multidomain SMAD proteins Computational and Structural Biotechnology Journal (2021)
Gomes T, Martin-Malpartida P, Ruiz L, Aragón E, Cordeiro T, Macias M
RgGuinier 5.2 nm
Dmax 20.0 nm

SASDLC2 – Mothers against decapentaplegic homolog 2, SMAD2 phosphomimetic mutant 1.5 mg/ml

Mothers against decapentaplegic homolog 2 (C-terminus phosphomimetic mutant) experimental SAS data
Mothers against decapentaplegic homolog 2 (C-terminus phosphomimetic mutant) Kratky plot
Sample: Mothers against decapentaplegic homolog 2 (C-terminus phosphomimetic mutant) , 53 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2016 Apr 4
Conformational landscape of multidomain SMAD proteins Computational and Structural Biotechnology Journal (2021)
Gomes T, Martin-Malpartida P, Ruiz L, Aragón E, Cordeiro T, Macias M
RgGuinier 5.3 nm
Dmax 20.0 nm

SASDLP2 – Outer membrane associated protein, FopA dimer in Tris-HCl, NaCl and n-Dodecyl beta-D-maltoside

Francisella tularensis outer membrane protein A experimental SAS data
Sample: Francisella tularensis outer membrane protein A dimer, 80 kDa Francisella tularensis subsp. … protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.05% B-DDM, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Mar 20
Structural and biophysical properties of FopA, a major outer membrane protein of Francisella tularensis. PLoS One 17(8):e0267370 (2022)
Nagaratnam N, Martin-Garcia JM, Yang JH, Goode MR, Ketawala G, Craciunescu FM, Zook JD, Sonowal M, Williams D, Grant TD, Fromme R, Hansen DT, Fromme P
RgGuinier 4.4 nm
Dmax 16.0 nm
VolumePorod 330 nm3

SASDHY2 – Human APPL2 (DCC-interacting protein 13-beta)

Adaptor protein, phosphotyrosine interaction, pleckstrin homology domain, and leucine zipper-containing protein 2 experimental SAS data
BUNCH model
Sample: Adaptor protein, phosphotyrosine interaction, pleckstrin homology domain, and leucine zipper-containing protein 2 dimer, 87 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, 5 mM MgCl2, 1 mM DTT, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 7 Apr 20
Membrane curvature protein exhibits interdomain flexibility and binds a small GTPase. J Biol Chem 287(49):40996-1006 (2012)
King GJ, Stöckli J, Hu SH, Winnen B, Duprez WG, Meoli CC, Junutula JR, Jarrott RJ, James DE, Whitten AE, Martin JL
RgGuinier 5.1 nm
Dmax 18.0 nm
VolumePorod 140 nm3

SASDHZ2 – 14-3-3 protein beta isoform

14-3-3 protein beta/alpha experimental SAS data
BUNCH model
Sample: 14-3-3 protein beta/alpha dimer, 58 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, and 2 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2011 Apr 7
The weak complex between RhoGAP protein ARHGAP22 and signal regulatory protein 14-3-3 has 1:2 stoichiometry and a single peptide binding mode. PLoS One 7(8):e41731 (2012)
Hu SH, Whitten AE, King GJ, Jones A, Rowland AF, James DE, Martin JL
RgGuinier 3.0 nm
Dmax 10.0 nm
VolumePorod 92 nm3

SASDH33 – Rho GTPase-activating protein 22

Rho GTPase-activating protein 22 experimental SAS data
BUNCH model
Sample: Rho GTPase-activating protein 22 monomer, 47 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, and 2 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2011 Apr 7
The weak complex between RhoGAP protein ARHGAP22 and signal regulatory protein 14-3-3 has 1:2 stoichiometry and a single peptide binding mode. PLoS One 7(8):e41731 (2012)
Hu SH, Whitten AE, King GJ, Jones A, Rowland AF, James DE, Martin JL
RgGuinier 3.2 nm
Dmax 12.0 nm
VolumePorod 88 nm3

SASDH83 – Chemically crossed linked complex between Rho GTPase-activating protein 22 (ARHGAP22) and the beta isoform of the 14-3-3 protein beta/alpha

14-3-3 protein beta/alphaRho GTPase-activating protein 22 experimental SAS data
CORAL model
Sample: 14-3-3 protein beta/alpha dimer, 58 kDa Homo sapiens protein
Rho GTPase-activating protein 22 monomer, 47 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, and 2 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2011 Apr 7
The weak complex between RhoGAP protein ARHGAP22 and signal regulatory protein 14-3-3 has 1:2 stoichiometry and a single peptide binding mode. PLoS One 7(8):e41731 (2012)
Hu SH, Whitten AE, King GJ, Jones A, Rowland AF, James DE, Martin JL
RgGuinier 3.8 nm
Dmax 14.0 nm
VolumePorod 195 nm3

SASDU93 – multimodular GH16_3 containing a CBM and a catalytic domain

Glycosyl hydrolase, family 16 experimental SAS data
DADIMODO model
Sample: Glycosyl hydrolase, family 16 monomer, 58 kDa Christiangramia forsetii (strain … protein
Buffer: 10 mM MOPS, 100 mM NaCl, pH: 7.8
Experiment: SAXS data collected at SWING, SOLEIL on 2022 Dec 1
Unveiling the role of novel carbohydrate-binding modules in laminarin interaction of multimodular proteins from marine Bacteroidota during phytoplankton blooms. Environ Microbiol 26(5):e16624 (2024)
Zühlke MK, Ficko-Blean E, Bartosik D, Terrapon N, Jeudy A, Jam M, Wang F, Welsch N, Dürwald A, Martin LT, Larocque R, Jouanneau D, Eisenack T, Thomas F, Trautwein-Schult A, Teeling H, Becher D, Schwed...
RgGuinier 3.8 nm
Dmax 12.9 nm
VolumePorod 76 nm3

SASDUA3 – Surface glycan binding protein (Cf-SGBP) from Christiangramia forsetii

PKD domain-containing protein experimental SAS data
DADIMODO model
Sample: PKD domain-containing protein monomer, 96 kDa Christiangramia forsetii (strain … protein
Buffer: 10 mM MOPS, 100 mM NaCl, pH: 7.8
Experiment: SAXS data collected at SWING, SOLEIL on 2022 Dec 1
Unveiling the role of novel carbohydrate-binding modules in laminarin interaction of multimodular proteins from marine Bacteroidota during phytoplankton blooms. Environ Microbiol 26(5):e16624 (2024)
Zühlke MK, Ficko-Blean E, Bartosik D, Terrapon N, Jeudy A, Jam M, Wang F, Welsch N, Dürwald A, Martin LT, Larocque R, Jouanneau D, Eisenack T, Thomas F, Trautwein-Schult A, Teeling H, Becher D, Schwed...
RgGuinier 5.0 nm
Dmax 17.8 nm
VolumePorod 138 nm3

SASDMY3 – Lysozyme amyloid fibril (LAF)

lysozyme amyloid fibril experimental SAS data
DAMMIF model
Sample: lysozyme amyloid fibril , 1 kDa Gallus gallus protein
Buffer: 0.2 M glycine-HCl, 80 mM NaCl, pH: 2.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Nov 29
Dependence of the Nanoscale Composite Morphology of Fe3O4 Nanoparticle-Infused Lysozyme Amyloid Fibrils on Timing of Infusion: A Combined SAXS and AFM Study Molecules 26(16):4864 (2021)
Schroer M, Hu P, Tomasovicova N, Batkova M, Zakutanska K, Wu P, Kopcansky P
RgGuinier 38.4 nm
Dmax 80.0 nm

SASDMZ3 – Fe3O4 nanoparticles (10 nm diameter)

Fe3O4 nanoparticles; nominal diameter 10 nm (hydrodynamic diameter) experimental SAS data
Fe3O4 nanoparticles; nominal diameter 10 nm (hydrodynamic diameter) Kratky plot
Sample: Fe3O4 nanoparticles; nominal diameter 10 nm (hydrodynamic diameter) monomer, 1 kDa
Buffer: 50 mM borate buffer, 0.02% NaN3, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Nov 29
Dependence of the Nanoscale Composite Morphology of Fe3O4 Nanoparticle-Infused Lysozyme Amyloid Fibrils on Timing of Infusion: A Combined SAXS and AFM Study Molecules 26(16):4864 (2021)
Schroer M, Hu P, Tomasovicova N, Batkova M, Zakutanska K, Wu P, Kopcansky P
RgGuinier 7.0 nm
Dmax 8.0 nm

SASDM24 – Fe3O4 nanoparticles (20 nm diameter)

Fe3O4 nanoparticles; nominal diameter 20 nm (hydrodynamic diameter) experimental SAS data
Fe3O4 nanoparticles; nominal diameter 20 nm (hydrodynamic diameter) Kratky plot
Sample: Fe3O4 nanoparticles; nominal diameter 20 nm (hydrodynamic diameter) monomer, 1 kDa
Buffer: 50 mM borate buffer, 0.02% NaN3, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Nov 29
Dependence of the Nanoscale Composite Morphology of Fe3O4 Nanoparticle-Infused Lysozyme Amyloid Fibrils on Timing of Infusion: A Combined SAXS and AFM Study Molecules 26(16):4864 (2021)
Schroer M, Hu P, Tomasovicova N, Batkova M, Zakutanska K, Wu P, Kopcansky P
RgGuinier 11.0 nm
Dmax 14.0 nm

SASDM34 – Fe3O4 nanoparticles (30 nm diameter)

Fe3O4 nanoparticles; nominal diameter 30 nm (hydrodynamic diameter) experimental SAS data
Fe3O4 nanoparticles; nominal diameter 30 nm (hydrodynamic diameter) Kratky plot
Sample: Fe3O4 nanoparticles; nominal diameter 30 nm (hydrodynamic diameter) monomer, 1 kDa
Buffer: 50 mM borate buffer, 0.02% NaN3, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Nov 29
Dependence of the Nanoscale Composite Morphology of Fe3O4 Nanoparticle-Infused Lysozyme Amyloid Fibrils on Timing of Infusion: A Combined SAXS and AFM Study Molecules 26(16):4864 (2021)
Schroer M, Hu P, Tomasovicova N, Batkova M, Zakutanska K, Wu P, Kopcansky P
RgGuinier 18.1 nm
Dmax 16.9 nm

SASDM44 – LAF + P10 nanocomposite (NP added before fibrilization)

lysozyme amyloid fibrilFe3O4 nanoparticles; nominal diameter 10 nm (hydrodynamic diameter) experimental SAS data
DAMMIN model
Sample: lysozyme amyloid fibril , 1 kDa Gallus gallus protein
Fe3O4 nanoparticles; nominal diameter 10 nm (hydrodynamic diameter) monomer, 1 kDa
Buffer: 0.2 M glycine-HCl, 80 mM NaCl, pH: 2.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Nov 29
Dependence of the Nanoscale Composite Morphology of Fe3O4 Nanoparticle-Infused Lysozyme Amyloid Fibrils on Timing of Infusion: A Combined SAXS and AFM Study Molecules 26(16):4864 (2021)
Schroer M, Hu P, Tomasovicova N, Batkova M, Zakutanska K, Wu P, Kopcansky P
RgGuinier 22.3 nm
Dmax 70.0 nm

SASDM54 – LAF + P30 nanocomposite (NP added before fibrilization)

lysozyme amyloid fibrilFe3O4 nanoparticles; nominal diameter 30 nm (hydrodynamic diameter) experimental SAS data
DAMMIN model
Sample: lysozyme amyloid fibril , 1 kDa Gallus gallus protein
Fe3O4 nanoparticles; nominal diameter 30 nm (hydrodynamic diameter) monomer, 1 kDa
Buffer: 0.2 M glycine-HCl, 80 mM NaCl, pH: 2.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Nov 29
Dependence of the Nanoscale Composite Morphology of Fe3O4 Nanoparticle-Infused Lysozyme Amyloid Fibrils on Timing of Infusion: A Combined SAXS and AFM Study Molecules 26(16):4864 (2021)
Schroer M, Hu P, Tomasovicova N, Batkova M, Zakutanska K, Wu P, Kopcansky P
RgGuinier 22.5 nm
Dmax 95.0 nm

SASDM64 – LAF + P20 nanocomposite (NP added before fibrilization)

lysozyme amyloid fibrilFe3O4 nanoparticles; nominal diameter 20 nm (hydrodynamic diameter) experimental SAS data
DAMMIN model
Sample: lysozyme amyloid fibril , 1 kDa Gallus gallus protein
Fe3O4 nanoparticles; nominal diameter 20 nm (hydrodynamic diameter) monomer, 1 kDa
Buffer: 0.2 M glycine-HCl, 80 mM NaCl, pH: 2.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Nov 29
Dependence of the Nanoscale Composite Morphology of Fe3O4 Nanoparticle-Infused Lysozyme Amyloid Fibrils on Timing of Infusion: A Combined SAXS and AFM Study Molecules 26(16):4864 (2021)
Schroer M, Hu P, Tomasovicova N, Batkova M, Zakutanska K, Wu P, Kopcansky P
RgGuinier 23.6 nm
Dmax 90.0 nm

SASDM74 – LAF + P20 nanocomposite (NP added after fibrilization)

lysozyme amyloid fibrilFe3O4 nanoparticles; nominal diameter 20 nm (hydrodynamic diameter) experimental SAS data
DAMMIN model
Sample: lysozyme amyloid fibril , 1 kDa Gallus gallus protein
Fe3O4 nanoparticles; nominal diameter 20 nm (hydrodynamic diameter) monomer, 1 kDa
Buffer: 0.2 M glycine-HCl, 80 mM NaCl, pH: 2.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Sep 2
Dependence of the Nanoscale Composite Morphology of Fe3O4 Nanoparticle-Infused Lysozyme Amyloid Fibrils on Timing of Infusion: A Combined SAXS and AFM Study Molecules 26(16):4864 (2021)
Schroer M, Hu P, Tomasovicova N, Batkova M, Zakutanska K, Wu P, Kopcansky P
RgGuinier 31.0 nm
Dmax 75.0 nm

SASDB94 – Suppressor of Copper Sensitivity C protein (ScsC) from Proteus mirabilis

C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein experimental SAS data
Suppressor of Copper Sensitivity C protein (ScsC) from Proteus mirabilis Rg histogram
Sample: C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein monomer, 20 kDa Proteus mirabilis protein
Buffer: 25 mM HEPES 150mM NaCl 1mM DTT, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2012 Feb 29
A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance. Nat Commun 8:16065 (2017)
Furlong EJ, Lo AW, Kurth F, Premkumar L, Totsika M, Achard MES, Halili MA, Heras B, Whitten AE, Choudhury HG, Schembri MA, Martin JL
RgGuinier 3.7 nm
Dmax 10.5 nm
VolumePorod 92 nm3

SASDWF4 – Outer membrane protein MIP from Legionella pneumophila (LpMIP) in complex with inhibitor NJS224

Outer membrane protein MIP(2S)‐2‐{[(2S)‐1‐[(4‐ fluorophenyl)methanesulfonyl]piperidin‐2‐ yl]formamido}‐4‐methyl‐N‐[(pyridin‐3‐ yl)methyl]pentanamide experimental SAS data
SREFLEX model
Sample: Outer membrane protein MIP dimer, 46 kDa Legionella pneumophila subsp. … protein
(2S)‐2‐{[(2S)‐1‐[(4‐ fluorophenyl)methanesulfonyl]piperidin‐2‐ yl]formamido}‐4‐methyl‐N‐[(pyridin‐3‐ yl)methyl]pentanamide monomer, 1 kDa
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Nov 22
Structure and Dynamics of Macrophage Infectivity Potentiator Proteins from Pathogenic Bacteria and Protozoans Bound to Fluorinated Pipecolic Acid Inhibitors. J Med Chem (2025)
Pérez Carrillo VH, Whittaker JJ, Wiedemann C, Harder JM, Lohr T, Jamithireddy AK, Dajka M, Goretzki B, Joseph B, Guskov A, Harmer NJ, Holzgrabe U, Hellmich UA
RgGuinier 2.9 nm
Dmax 9.7 nm
VolumePorod 61 nm3

SASDWG4 – Outer membrane protein MIP from Legionella pneumophila (LpMIP) in complex with inhibitor NJS227

Outer membrane protein MIP(2S)‐3‐(4‐fluorophenyl)‐2‐{[(2S)‐1‐[(4‐ fluorophenyl)methanesulfonyl]piperidin‐2‐ yl]formamido}‐N‐[(pyridin‐3‐yl)methyl]propanamide experimental SAS data
SREFLEX model
Sample: Outer membrane protein MIP dimer, 46 kDa Legionella pneumophila subsp. … protein
(2S)‐3‐(4‐fluorophenyl)‐2‐{[(2S)‐1‐[(4‐ fluorophenyl)methanesulfonyl]piperidin‐2‐ yl]formamido}‐N‐[(pyridin‐3‐yl)methyl]propanamide monomer, 1 kDa
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Nov 22
Structure and Dynamics of Macrophage Infectivity Potentiator Proteins from Pathogenic Bacteria and Protozoans Bound to Fluorinated Pipecolic Acid Inhibitors. J Med Chem (2025)
Pérez Carrillo VH, Whittaker JJ, Wiedemann C, Harder JM, Lohr T, Jamithireddy AK, Dajka M, Goretzki B, Joseph B, Guskov A, Harmer NJ, Holzgrabe U, Hellmich UA
RgGuinier 3.0 nm
Dmax 10.0 nm
VolumePorod 65 nm3

SASDMJ4 – Lysozyme amyloid fibril (LAF)

lysozyme amyloid fibril experimental SAS data
DAMMIF model
Sample: lysozyme amyloid fibril , 14 kDa Gallus gallus protein
Buffer: 0.2 M glycine-HCl, 80 mM NaCl, pH: 2.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Sep 5
Effect of the concentration of protein and nanoparticles on the structure of biohybrid nanocomposites. Biopolymers 111(2):e23342 (2020)
Majorošová J, Schroer MA, Tomašovičová N, Batková M, Hu PS, Kubovčíková M, Svergun DI, Kopčanský P
RgGuinier 30.2 nm
Dmax 120.0 nm

SASDMK4 – Fe3O4 nanoparticles (radius 5.6 nm )

Fe3O4 nanoparticles; radius 5.6 nm (AFM based) experimental SAS data
Fe3O4 nanoparticles; radius 5.6 nm (AFM based) Kratky plot
Sample: Fe3O4 nanoparticles; radius 5.6 nm (AFM based) monomer, 1 kDa
Buffer: water, HCLO4, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Sep 5
Effect of the concentration of protein and nanoparticles on the structure of biohybrid nanocomposites. Biopolymers 111(2):e23342 (2020)
Majorošová J, Schroer MA, Tomašovičová N, Batková M, Hu PS, Kubovčíková M, Svergun DI, Kopčanský P
RgGuinier 11.0 nm
Dmax 20.0 nm

SASDML4 – LAF + MNP (r = 5.6 nm) nanocomposite

lysozyme amyloid fibrilFe3O4 nanoparticles; radius 5.6 nm (AFM based) experimental SAS data
DAMMIF model
Sample: lysozyme amyloid fibril , 1 kDa Gallus gallus protein
Fe3O4 nanoparticles; radius 5.6 nm (AFM based) monomer, 1 kDa
Buffer: 0.2 M glycine-HCl, 80 mM NaCl, pH: 2.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Sep 8
Effect of the concentration of protein and nanoparticles on the structure of biohybrid nanocomposites. Biopolymers 111(2):e23342 (2020)
Majorošová J, Schroer MA, Tomašovičová N, Batková M, Hu PS, Kubovčíková M, Svergun DI, Kopčanský P
RgGuinier 29.4 nm
Dmax 80.0 nm

SASDCY4 – RNase E 603-850

RNase E 603-850 experimental SAS data
RNase E 603-850 Rg histogram
Sample: RNase E 603-850 monomer, 30 kDa Escherichia coli protein
Buffer: 50 mM Tris HCl, 100 mM NaCl, 100 mM KCl, 10 mM MgCl2, 10 mM DTT and 5 % glycerol (v/v), pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2014 Dec 5
Analysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes. Nucleic Acids Res 46(1):387-402 (2018)
Bruce HA, Du D, Matak-Vinkovic D, Bandyra KJ, Broadhurst RW, Martin E, Sobott F, Shkumatov AV, Luisi BF
RgGuinier 5.3 nm
Dmax 27.5 nm
VolumePorod 139 nm3

SASDCZ4 – RNase E 603-850/ATP-dependent RNA helicase (RhlB) binary complex

RNase E 603-850ATP-dependent RNA helicase RhlB experimental SAS data
GASBOR model
Sample: RNase E 603-850 monomer, 30 kDa Escherichia coli protein
ATP-dependent RNA helicase RhlB monomer, 47 kDa Escherichia coli protein
Buffer: 50 mM Tris HCl, 100 mM NaCl, 100 mM KCl, 10 mM MgCl2, 10 mM DTT and 5 % glycerol (v/v), pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2016 Feb 11
Analysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes. Nucleic Acids Res 46(1):387-402 (2018)
Bruce HA, Du D, Matak-Vinkovic D, Bandyra KJ, Broadhurst RW, Martin E, Sobott F, Shkumatov AV, Luisi BF
RgGuinier 5.4 nm
Dmax 29.5 nm
VolumePorod 183 nm3

SASDC25 – RNase E 603-850/ATP-dependent RNA helicase (RhlB)/enolase ternary complex

RNase E 603-850ATP-dependent RNA helicase RhlBEnolase experimental SAS data
GASBOR model
Sample: RNase E 603-850 monomer, 30 kDa Escherichia coli protein
ATP-dependent RNA helicase RhlB monomer, 47 kDa Escherichia coli protein
Enolase dimer, 91 kDa Escherichia coli protein
Buffer: 50 mM Tris HCl, 100 mM NaCl, 100 mM KCl, 10 mM MgCl2, 10 mM DTT and 5 % glycerol (v/v), pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2014 Jul 16
Analysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes. Nucleic Acids Res 46(1):387-402 (2018)
Bruce HA, Du D, Matak-Vinkovic D, Bandyra KJ, Broadhurst RW, Martin E, Sobott F, Shkumatov AV, Luisi BF
RgGuinier 6.4 nm
Dmax 30.5 nm
VolumePorod 280 nm3

SASDJ85 – Zinc transporter 1 – hZnT1-CTD

Zinc transporter 1 experimental SAS data
DAMFILT model
Sample: Zinc transporter 1 dimer, 37 kDa Homo sapiens protein
Buffer: 20mM Tris, 150mM NaCl, 1mM TCEP, pH: 7.6
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Aug 14
Heterologous Expression and Biochemical Characterization of the Human Zinc Transporter 1 (ZnT1) and Its Soluble C-Terminal Domain Frontiers in Chemistry 9 (2021)
Cotrim C, Jarrott R, Whitten A, Choudhury H, Drew D, Martin J
RgGuinier 2.7 nm
Dmax 10.0 nm
VolumePorod 50 nm3

SASDFC5 – Enhanced disease susceptibility 1 (EDS1)

Enhanced disease susceptibility experimental SAS data
DAMMIN model
Sample: Enhanced disease susceptibility monomer, 72 kDa Arabidopsis thaliana protein
Buffer: 50 mM NaCl, 50 mM HEPES, 1% glyercol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2015 May 19
Arabidopsis immunity regulator EDS1 in a PAD4/SAG101-unbound form is a monomer with an inherently inactive conformation. J Struct Biol :107390 (2019)
Voss M, Toelzer C, Bhandari DD, Parker JE, Niefind K
RgGuinier 3.1 nm
Dmax 10.5 nm
VolumePorod 92 nm3

SASDLL5 – frataxin homolog, Yfh1, at 0 °C

Frataxin homolog, mitochondrial experimental SAS data
frataxin homolog, Yfh1, at 0 °C Rg histogram
Sample: Frataxin homolog, mitochondrial monomer, 14 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 20 mM HEPES, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Nov 28
The role of hydration in protein stability: comparison of the cold and heat unfolded states of Yfh1. J Mol Biol 417(5):413-24 (2012)
Adrover M, Martorell G, Martin SR, Urosev D, Konarev PV, Svergun DI, Daura X, Temussi P, Pastore A
RgGuinier 2.2 nm

SASDLM5 – frataxin homolog, Yfh1, at 20 °C

Frataxin homolog, mitochondrial experimental SAS data
frataxin homolog, Yfh1, at 20 °C Rg histogram
Sample: Frataxin homolog, mitochondrial monomer, 14 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 20 mM HEPES, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Nov 28
The role of hydration in protein stability: comparison of the cold and heat unfolded states of Yfh1. J Mol Biol 417(5):413-24 (2012)
Adrover M, Martorell G, Martin SR, Urosev D, Konarev PV, Svergun DI, Daura X, Temussi P, Pastore A
RgGuinier 2.1 nm

SASDLN5 – frataxin homolog, Yfh1, at 50 °C

Frataxin homolog, mitochondrial experimental SAS data
frataxin homolog, Yfh1, at 50 °C Rg histogram
Sample: Frataxin homolog, mitochondrial monomer, 14 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 20 mM HEPES, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Nov 28
The role of hydration in protein stability: comparison of the cold and heat unfolded states of Yfh1. J Mol Biol 417(5):413-24 (2012)
Adrover M, Martorell G, Martin SR, Urosev D, Konarev PV, Svergun DI, Daura X, Temussi P, Pastore A
RgGuinier 2.5 nm

SASDP46 – Glycoside Hydrolase Family 5 endo-mannanase retrieved from Capybara gut metagenome

GH5 endo-mannanase from Capybara gut metagenome experimental SAS data
PYMOL model
Sample: GH5 endo-mannanase from Capybara gut metagenome monomer, 46 kDa metagenome protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2018 Oct 30
Glycoside hydrolase subfamily GH5_57 features a highly redesigned catalytic interface to process complex hetero-β-mannans. Acta Crystallogr D Struct Biol 78(Pt 11):1358-1372 (2022)
Martins MP, Morais MAB, Persinoti GF, Galinari RH, Yu L, Yoshimi Y, Passos Nunes FB, Lima TB, Barbieri SF, Silveira JLM, Lombard V, Terrapon N, Dupree P, Henrissat B, Murakami MT
RgGuinier 2.3 nm
Dmax 5.5 nm
VolumePorod 58 nm3

SASDHC6 – C-terminal domain-like carotenoid protein (CCP2), apo-dimer

C-terminal domain-like carotenoid protein experimental SAS data
BILBOMD model
Sample: C-terminal domain-like carotenoid protein dimer, 33 kDa Tolypothrix sp. PCC … protein
Buffer: 10 mM potassium phosphate, 100 mM NaCl, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 15
Structural analysis of a new carotenoid-binding protein: the C-terminal domain homolog of the OCP Scientific Reports 10(1) (2020)
Dominguez-Martin M, Hammel M, Gupta S, Lechno-Yossef S, Sutter M, Rosenberg D, Chen Y, Petzold C, Ralston C, Polívka T, Kerfeld C
RgGuinier 2.5 nm
Dmax 9.1 nm
VolumePorod 55 nm3

SASDHD6 – C-terminal domain-like carotenoid protein (CCP2), holo-dimer

C-terminal domain-like carotenoid protein experimental SAS data
BILBOMD model
Sample: C-terminal domain-like carotenoid protein dimer, 36 kDa Tolypothrix sp. PCC … protein
Buffer: 10 mM potassium phosphate, 100 mM NaCl, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 15
Structural analysis of a new carotenoid-binding protein: the C-terminal domain homolog of the OCP Scientific Reports 10(1) (2020)
Dominguez-Martin M, Hammel M, Gupta S, Lechno-Yossef S, Sutter M, Rosenberg D, Chen Y, Petzold C, Ralston C, Polívka T, Kerfeld C
RgGuinier 2.5 nm
Dmax 7.9 nm
VolumePorod 62 nm3

SASDHE6 – C-terminal domain-like carotenoid protein (CCP2), apo-tetramer

C-terminal domain-like carotenoid protein experimental SAS data
BILBOMD model
Sample: C-terminal domain-like carotenoid protein tetramer, 66 kDa Tolypothrix sp. PCC … protein
Buffer: 10 mM potassium phosphate, 100 mM NaCl, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 15
Structural analysis of a new carotenoid-binding protein: the C-terminal domain homolog of the OCP Scientific Reports 10(1) (2020)
Dominguez-Martin M, Hammel M, Gupta S, Lechno-Yossef S, Sutter M, Rosenberg D, Chen Y, Petzold C, Ralston C, Polívka T, Kerfeld C
RgGuinier 3.2 nm
Dmax 10.0 nm
VolumePorod 110 nm3

SASDHF6 – C-terminal domain-like carotenoid protein (CCP2), holo-tetramer

C-terminal domain-like carotenoid protein experimental SAS data
BILBOMD model
Sample: C-terminal domain-like carotenoid protein tetramer, 73 kDa Tolypothrix sp. PCC … protein
Buffer: 10 mM potassium phosphate, 100 mM NaCl, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 15
Structural analysis of a new carotenoid-binding protein: the C-terminal domain homolog of the OCP Scientific Reports 10(1) (2020)
Dominguez-Martin M, Hammel M, Gupta S, Lechno-Yossef S, Sutter M, Rosenberg D, Chen Y, Petzold C, Ralston C, Polívka T, Kerfeld C
RgGuinier 3.3 nm
Dmax 12.1 nm
VolumePorod 157 nm3

SASDAV6 – Cysteine desulfurase IscS dimer

Cysteine desulfurase IscS experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Cysteine desulfurase IscS dimer, 87 kDa Escherichia coli protein
Buffer: 20 mM Tris-HCl 150 mM NaCl 10 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 5
Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. Nat Commun 1:95 (2010)
Prischi F, Konarev PV, Iannuzzi C, Pastore C, Adinolfi S, Martin SR, Svergun DI, Pastore A
RgGuinier 3.2 nm
Dmax 10.9 nm

SASDAW6 – Iron-sulfur cluster assembly scaffold IscU monomer

Iron-sulfur cluster assembly scaffold protein IscU experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Iron-sulfur cluster assembly scaffold protein IscU monomer, 14 kDa Escherichia coli protein
Buffer: 20 mM Tris-HCl 150 mM NaCl 10 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 5
Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. Nat Commun 1:95 (2010)
Prischi F, Konarev PV, Iannuzzi C, Pastore C, Adinolfi S, Martin SR, Svergun DI, Pastore A
RgGuinier 1.9 nm
Dmax 6.4 nm

SASDBW6 – Suppressor of Copper Sensitivity C protein (ScsC) from P. mirabilis (mutant)

Suppressor of Copper Sensitivity C protein (mutant) experimental SAS data
Suppressor of Copper Sensitivity C protein (ScsC) from P. mirabilis (mutant) Rg histogram
Sample: Suppressor of Copper Sensitivity C protein (mutant) trimer, 73 kDa Proteus mirabilis protein
Buffer: 25 mM HEPES 150mM NaCl, 1mM DTT,, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2016 Jul 22
A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance. Nat Commun 8:16065 (2017)
Furlong EJ, Lo AW, Kurth F, Premkumar L, Totsika M, Achard MES, Halili MA, Heras B, Whitten AE, Choudhury HG, Schembri MA, Martin JL
RgGuinier 4.4 nm
Dmax 13.5 nm
VolumePorod 108 nm3

SASDAX6 – Protein CyaY monomer

Protein CyaY experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Protein CyaY monomer, 12 kDa Escherichia coli protein
Buffer: 20 mM Tris-HCl 150 mM NaCl 10 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 5
Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. Nat Commun 1:95 (2010)
Prischi F, Konarev PV, Iannuzzi C, Pastore C, Adinolfi S, Martin SR, Svergun DI, Pastore A
RgGuinier 1.5 nm
Dmax 5.0 nm

SASDAY6 – IcsS-dimer and IscU-dimer complex

Cysteine desulfurase IscSIron-sulfur cluster assembly scaffold protein IscU experimental SAS data
DAMMIF model
Sample: Cysteine desulfurase IscS dimer, 87 kDa Escherichia coli protein
Iron-sulfur cluster assembly scaffold protein IscU dimer, 29 kDa Escherichia coli protein
Buffer: 20 mM Tris-HCl 150 mM NaCl 10 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 5
Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. Nat Commun 1:95 (2010)
Prischi F, Konarev PV, Iannuzzi C, Pastore C, Adinolfi S, Martin SR, Svergun DI, Pastore A
RgGuinier 3.6 nm
Dmax 12.1 nm

SASDAZ6 – CyaY-dimer and IscS-dimer complex

Cysteine desulfurase IscSProtein CyaY experimental SAS data
SASREF model
Sample: Cysteine desulfurase IscS dimer, 87 kDa Escherichia coli protein
Protein CyaY dimer, 24 kDa Escherichia coli protein
Buffer: 20 mM Tris-HCl, 50 mM NaCl, 10 mM β-mercaptoethanol and ferrous ammonium sulphate, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 5
Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. Nat Commun 1:95 (2010)
Prischi F, Konarev PV, Iannuzzi C, Pastore C, Adinolfi S, Martin SR, Svergun DI, Pastore A
RgGuinier 3.1 nm
Dmax 10.9 nm

SASDA27 – IcsS, IscU and CyaY dimeric complex

Cysteine desulfurase IscSIron-sulfur cluster assembly scaffold protein IscUProtein CyaY experimental SAS data
SASREF model
Sample: Cysteine desulfurase IscS dimer, 87 kDa Escherichia coli protein
Iron-sulfur cluster assembly scaffold protein IscU dimer, 29 kDa Escherichia coli protein
Protein CyaY dimer, 24 kDa Escherichia coli protein
Buffer: 20 mM Tris-HCl 150 mM NaCl 10 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 5
Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. Nat Commun 1:95 (2010)
Prischi F, Konarev PV, Iannuzzi C, Pastore C, Adinolfi S, Martin SR, Svergun DI, Pastore A
RgGuinier 3.5 nm
Dmax 11.9 nm

SASDL47 – Oligomeric composition of AXH Domain of Ataxin-1 (wild type and A567G, I580A mutants)

Ataxin-1 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Ataxin-1 monomer, 14 kDa Homo sapiens protein
Buffer: 20 mM Tris-HCl, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Oct 21
Self-assembly and conformational heterogeneity of the AXH domain of ataxin-1: an unusual example of a chameleon fold. Biophys J 104(6):1304-13 (2013)
de Chiara C, Rees M, Menon RP, Pauwels K, Lawrence C, Konarev PV, Svergun DI, Martin SR, Chen YW, Pastore A
RgGuinier 5.5 nm

SASDJL7 – Oxidised fimbrial BcfH protein

Hypothetical exported protein experimental SAS data
CORAL model
Sample: Hypothetical exported protein trimer, 83 kDa Salmonella typhimurium (strain … protein
Buffer: 25 mM TRIS, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Aug 14
Salmonella enterica BcfH is a trimeric thioredoxin-like bifunctional enzyme with both thiol oxidase and disulfide isomerase activities. Antioxid Redox Signal (2021)
Subedi P, Paxman JJ, Wang G, Hor L, Hong Y, Verderosa AD, Whitten AE, Panjikar S, Santos-Martin CF, Martin JL, Totsika M, Heras B
RgGuinier 3.2 nm
Dmax 11.5 nm
VolumePorod 93 nm3

SASDPV7 – FAD-dependent monooxygenase from Stenotrophomonas maltophilia (no reducing agent)

Monooxygenase (M154I, A283T) experimental SAS data
REFMAC model
Sample: Monooxygenase (M154I, A283T) monomer, 39 kDa Stenotrophomonas maltophilia protein
Buffer: 25 mM Bis-Tris, 150 mM NaCl, pH: 6.5
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Jan 10
Tetracycline-modifying enzyme Sm TetX from Stenotrophomonas maltophilia Acta Crystallographica Section F Structural Biology Communications 79(7):180-192 (2023)
Malý M, Kolenko P, Stránský J, Švecová L, Dušková J, Koval' T, Skálová T, Trundová M, Adámková K, Černý J, Božíková P, Dohnálek J
RgGuinier 2.4 nm
Dmax 6.8 nm
VolumePorod 59 nm3

SASDRV7 – SARS-CoV-2 5' untranslated region stem-loop 4 RNA (5_SL4) in phosphate buffer

stem-loop 4 from SARS-CoV-2 5'-UTR experimental SAS data
stem-loop 4 from SARS-CoV-2 5'-UTR Kratky plot
Sample: stem-loop 4 from SARS-CoV-2 5'-UTR monomer, 14 kDa SARS coronavirus 2-Wuhan RNA
Buffer: 25 mM potassium phosphate pH 6.5, 150 mM KCl, 2 mM TCEP, pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Aug 7
High-resolution structure of stem-loop 4 from the 5'-UTR of SARS-CoV-2 solved by solution state NMR. Nucleic Acids Res (2023)
...Martins J, Ferner J, Jonker HRA, Hargrove AE, Weigand JE, Wacker A, Schwalbe H, Wöhnert J, Duchardt-Ferner E
RgGuinier 2.1 nm
Dmax 7.0 nm
VolumePorod 22 nm3

SASDPW7 – FAD-dependent monooxygenase from Stenotrophomonas maltophilia (with reducing agent)

Monooxygenase (M154I, A283T) experimental SAS data
REFMAC model
Sample: Monooxygenase (M154I, A283T) monomer, 39 kDa Stenotrophomonas maltophilia protein
Buffer: 25 mM Bis-Tris, 150 mM NaCl, 30 mM DTT, pH: 6.5
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Jan 7
Tetracycline-modifying enzyme Sm TetX from Stenotrophomonas maltophilia Acta Crystallographica Section F Structural Biology Communications 79(7):180-192 (2023)
Malý M, Kolenko P, Stránský J, Švecová L, Dušková J, Koval' T, Skálová T, Trundová M, Adámková K, Černý J, Božíková P, Dohnálek J
RgGuinier 2.4 nm
Dmax 6.4 nm
VolumePorod 64 nm3

SASDC28 – Mature α-DsbA2 protein

DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) experimental SAS data
DAMMIN model
Sample: DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) trimer, 81 kDa Wolbachia endosymbiont of … protein
Buffer: 25 mM TRIS, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2014 Mar 29
The atypical thiol-disulfide exchange protein α-DsbA2 from Wolbachia pipientis is a homotrimeric disulfide isomerase. Acta Crystallogr D Struct Biol 75(Pt 3):283-295 (2019)
Walden PM, Whitten AE, Premkumar L, Halili MA, Heras B, King GJ, Martin JL
RgGuinier 2.8 nm
Dmax 8.7 nm
VolumePorod 913 nm3

SASDC38 – Truncated α-DsbA2 protein

DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) experimental SAS data
DAMMIN model
Sample: DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) monomer, 21 kDa Wolbachia endosymbiont of … protein
Buffer: 25 mM TRIS, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2012 Feb 29
The atypical thiol-disulfide exchange protein α-DsbA2 from Wolbachia pipientis is a homotrimeric disulfide isomerase. Acta Crystallogr D Struct Biol 75(Pt 3):283-295 (2019)
Walden PM, Whitten AE, Premkumar L, Halili MA, Heras B, King GJ, Martin JL
RgGuinier 1.9 nm
Dmax 6.3 nm
VolumePorod 275 nm3

SASDC48 – ScsC-ScsBalpha complex

DsbA-like proteinPutative metal resistance protein experimental SAS data
SASREF model
Sample: DsbA-like protein trimer, 74 kDa Proteus mirabilis protein
Putative metal resistance protein monomer, 30 kDa Proteus mirabilis protein
Buffer: 10mM HEPES, 150mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2016 Nov 2
Disulfide isomerase activity of the dynamic, trimeric Proteus mirabilis ScsC protein is primed by the tandem immunoglobulin-fold domain of ScsB. J Biol Chem 293(16):5793-5805 (2018)
Furlong EJ, Choudhury HG, Kurth F, Duff AP, Whitten AE, Martin JL
RgGuinier 3.9 nm
Dmax 11.5 nm
VolumePorod 145 nm3

SASDQ78 – YbiB-ObgE GTPase complex

Uncharacterized protein YbiBGTPase Obg experimental SAS data
Uncharacterized protein YbiB GTPase Obg Kratky plot
Sample: Uncharacterized protein YbiB dimer, 75 kDa Escherichia coli (strain … protein
GTPase Obg dimer, 91 kDa Escherichia coli (strain … protein
Buffer: 20 mM HEPES, 150 mM NaCl, 5 mM MgCl2, 2 mM DTT, 5% glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Oct 24
YbiB: a novel interactor of the GTPase ObgE. Nucleic Acids Res (2023)
Deckers B, Vercauteren S, De Kock V, Martin C, Lazar T, Herpels P, Dewachter L, Verstraeten N, Peeters E, Ballet S, Michiels J, Galicia C, Versées W
RgGuinier 4.7 nm
Dmax 18.6 nm
VolumePorod 291 nm3

SASDFK8 – GON7, the fifth subunit of human KEOPS

EKC/KEOPS complex subunit GON7 experimental SAS data
EKC/KEOPS complex subunit GON7 Kratky plot
Sample: EKC/KEOPS complex subunit GON7 monomer, 13 kDa Homo sapiens protein
Buffer: 20 mM MES, 200 mM NaCl, 5 mM β-mercaptoethanol, pH: 6.5
Experiment: SAXS data collected at SWING, SOLEIL on 2017 Mar 26
Defects in t6A tRNA modification due to GON7 and YRDC mutations lead to Galloway-Mowat syndrome. Nat Commun 10(1):3967 (2019)
Arrondel C, Missoury S, Snoek R, Patat J, Menara G, Collinet B, Liger D, Durand D, Gribouval O, Boyer O, Buscara L, Martin G, Machuca E, Nevo F, Lescop E, Braun DA, Boschat AC, Sanquer S, Guerrera IC,...
RgGuinier 3.1 nm
Dmax 12.5 nm
VolumePorod 46 nm3

SASDFL8 – GON7, the fifth subunit of human KEOPS, bound to LAGE3-OSGEP (EKC/KEOPS complex subunit:Probable tRNA N6-adenosine threonylcarbamoyltransferase)

EKC/KEOPS complex subunit GON7EKC/KEOPS complex subunit LAGE3Probable tRNA N6-adenosine threonylcarbamoyltransferase experimental SAS data
OTHER model
Sample: EKC/KEOPS complex subunit GON7 monomer, 12 kDa Homo sapiens protein
EKC/KEOPS complex subunit LAGE3 monomer, 15 kDa Homo sapiens protein
Probable tRNA N6-adenosine threonylcarbamoyltransferase monomer, 36 kDa Homo sapiens protein
Buffer: 20 mM MES, 200 mM NaCl, 5 mM β-mercaptoethanol, pH: 6.5
Experiment: SAXS data collected at SWING, SOLEIL on 2017 May 12
Defects in t6A tRNA modification due to GON7 and YRDC mutations lead to Galloway-Mowat syndrome. Nat Commun 10(1):3967 (2019)
Arrondel C, Missoury S, Snoek R, Patat J, Menara G, Collinet B, Liger D, Durand D, Gribouval O, Boyer O, Buscara L, Martin G, Machuca E, Nevo F, Lescop E, Braun DA, Boschat AC, Sanquer S, Guerrera IC,...
RgGuinier 3.1 nm
Dmax 11.5 nm
VolumePorod 91 nm3

SASDHL8 – Aquifex aeolicus McoA metaloxidase evolved variant (2F4)

McoA evolved variant 2F4 (Periplasmic cell division protein (SufI)) experimental SAS data
OTHER model
Sample: McoA evolved variant 2F4 (Periplasmic cell division protein (SufI)) monomer, 55 kDa Aquifex aeolicus VF5 protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2017 Sep 25
Distal Mutations Shape Substrate-Binding Sites during Evolution of a Metallo-Oxidase into a Laccase ACS Catalysis :5022-5035 (2022)
...Martins L
RgGuinier 2.3 nm
Dmax 6.8 nm
VolumePorod 78 nm3

SASDFM8 – GON7, the fifth subunit of human KEOPS, bound to the EKC/KEOPS complex subunit, LAGE3

EKC/KEOPS complex subunit GON7EKC/KEOPS complex subunit LAGE3 experimental SAS data
EKC/KEOPS complex subunit GON7 EKC/KEOPS complex subunit LAGE3 Kratky plot
Sample: EKC/KEOPS complex subunit GON7 dimer, 25 kDa Homo sapiens protein
EKC/KEOPS complex subunit LAGE3 dimer, 33 kDa Homo sapiens protein
Buffer: 20 mM MES, 200 mM NaCl, 5 mM β-mercaptoethanol, pH: 6.5
Experiment: SAXS data collected at SWING, SOLEIL on 2017 Mar 19
Defects in t6A tRNA modification due to GON7 and YRDC mutations lead to Galloway-Mowat syndrome. Nat Commun 10(1):3967 (2019)
Arrondel C, Missoury S, Snoek R, Patat J, Menara G, Collinet B, Liger D, Durand D, Gribouval O, Boyer O, Buscara L, Martin G, Machuca E, Nevo F, Lescop E, Braun DA, Boschat AC, Sanquer S, Guerrera IC,...
RgGuinier 3.6 nm
Dmax 15.5 nm
VolumePorod 126 nm3

SASDHM8 – Aquifex aeolicus McoA metaloxidase ∆328-352 evolved variant (2F4∆328-352)

Aquifex aeolicus McoA metaloxidase ∆328-352 evolved variant (2F4∆328-352) experimental SAS data
DAMMIF model
Sample: Aquifex aeolicus McoA metaloxidase ∆328-352 evolved variant (2F4∆328-352) monomer, 53 kDa Aquifex aeolicus protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Jul 18
Distal Mutations Shape Substrate-Binding Sites during Evolution of a Metallo-Oxidase into a Laccase ACS Catalysis :5022-5035 (2022)
...Martins L
RgGuinier 2.2 nm
Dmax 6.6 nm
VolumePorod 74 nm3

SASDWN8 – β-Lactoglobulin A at 17.4 µM (pH 7.0)

Beta-lactoglobulin experimental SAS data
Beta-lactoglobulin Kratky plot
Sample: Beta-lactoglobulin , 20 kDa Bos taurus protein
Buffer: 20 mM MOPS, 100 mM NaCl, 1 mM TCEP, pH:
Experiment: SAXS data collected at BM29, ESRF on 2021 Nov 21
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 1.9 nm
Dmax 6.0 nm
VolumePorod 31 nm3

SASDWP8 – β-Lactoglobulin A at 26.1 µM (pH 7.0)

Beta-lactoglobulin experimental SAS data
Beta-lactoglobulin Kratky plot
Sample: Beta-lactoglobulin , 20 kDa Bos taurus protein
Buffer: 20 mM MOPS, 100 mM NaCl, 1 mM TCEP, pH:
Experiment: SAXS data collected at BM29, ESRF on 2021 Nov 21
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 2.0 nm
Dmax 8.5 nm
VolumePorod 30 nm3

SASDWQ8 – β-Lactoglobulin A at 34.8 µM (pH 7.0)

Beta-lactoglobulin experimental SAS data
Beta-lactoglobulin Kratky plot
Sample: Beta-lactoglobulin , 20 kDa Bos taurus protein
Buffer: 20 mM MOPS, 100 mM NaCl, 1 mM TCEP, pH:
Experiment: SAXS data collected at BM29, ESRF on 2021 Nov 21
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 2.0 nm
Dmax 8.5 nm
VolumePorod 33 nm3

SASDWR8 – β-Lactoglobulin A at 52.2 µM (pH 7.0)

Beta-lactoglobulin experimental SAS data
Beta-lactoglobulin Kratky plot
Sample: Beta-lactoglobulin , 20 kDa Bos taurus protein
Buffer: 20 mM MOPS, 100 mM NaCl, 1 mM TCEP, pH:
Experiment: SAXS data collected at BM29, ESRF on 2021 Nov 21
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 2.1 nm
Dmax 9.0 nm
VolumePorod 40 nm3

SASDWS8 – β-Lactoglobulin A at 69.6 µM (pH 7.0)

Beta-lactoglobulin experimental SAS data
Beta-lactoglobulin Kratky plot
Sample: Beta-lactoglobulin , 20 kDa Bos taurus protein
Buffer: 20 mM MOPS, 100 mM NaCl, 1 mM TCEP, pH:
Experiment: SAXS data collected at BM29, ESRF on 2021 Nov 21
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 2.1 nm
Dmax 9.0 nm
VolumePorod 44 nm3

SASDWT8 – β-Lactoglobulin A at 78.3 µM (pH 7.0)

Beta-lactoglobulin experimental SAS data
Beta-lactoglobulin Kratky plot
Sample: Beta-lactoglobulin , 20 kDa Bos taurus protein
Buffer: 20 mM MOPS, 100 mM NaCl, 1 mM TCEP, pH:
Experiment: SAXS data collected at BM29, ESRF on 2021 Nov 21
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 2.1 nm
Dmax 10.0 nm
VolumePorod 45 nm3

SASDTU8 – Complement C3* at 1.25 mg/mL (pH 6.0, 200 mM NaCl)

Complement C3 (Δ668-671) experimental SAS data
CORAL model
Sample: Complement C3 (Δ668-671) monomer, 187 kDa Homo sapiens protein
Buffer: 20 mM MES pH 6.0, 200 mM NaCl, pH: 6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2022 Nov 7
Cryo-EM analysis of complement C3 reveals a reversible major opening of the macroglobulin ring. Nat Struct Mol Biol (2025)
Gadeberg TAF, Jørgensen MH, Olesen HG, Lorentzen J, Harwood SL, Almeida AV, Fruergaard MU, Jensen RK, Kanis P, Pedersen H, Tranchant E, Petersen SV, Thøgersen IB, Kragelund BB, Lyons JA, Enghild JJ, A...
RgGuinier 5.4 nm
Dmax 21.8 nm
VolumePorod 357 nm3

SASDWU8 – β-Lactoglobulin A at 104.3 µM (pH 7.0)

Beta-lactoglobulin experimental SAS data
Beta-lactoglobulin Kratky plot
Sample: Beta-lactoglobulin , 20 kDa Bos taurus protein
Buffer: 20 mM MOPS, 100 mM NaCl, 1 mM TCEP, pH:
Experiment: SAXS data collected at BM29, ESRF on 2021 Nov 21
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 2.1 nm
Dmax 9.5 nm
VolumePorod 47 nm3

SASDWV8 – β-Lactoglobulin A at 130.4 µM (pH 7.0)

Beta-lactoglobulin experimental SAS data
Beta-lactoglobulin Kratky plot
Sample: Beta-lactoglobulin , 20 kDa Bos taurus protein
Buffer: 20 mM MOPS, 100 mM NaCl, 1 mM TCEP, pH:
Experiment: SAXS data collected at BM29, ESRF on 2021 Nov 21
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 2.1 nm
Dmax 10.0 nm
VolumePorod 49 nm3

SASDWW8 – β-Lactoglobulin A at 156.5 µM (pH 7.0)

Beta-lactoglobulin experimental SAS data
Beta-lactoglobulin Kratky plot
Sample: Beta-lactoglobulin , 20 kDa Bos taurus protein
Buffer: 20 mM MOPS, 100 mM NaCl, 1 mM TCEP, pH:
Experiment: SAXS data collected at BM29, ESRF on 2021 Nov 21
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 2.2 nm
Dmax 10.5 nm
VolumePorod 51 nm3

SASDWX8 – β-Lactoglobulin A at 260.9 µM (pH 7.0)

Beta-lactoglobulin experimental SAS data
Beta-lactoglobulin Kratky plot
Sample: Beta-lactoglobulin , 20 kDa Bos taurus protein
Buffer: 20 mM MOPS, 100 mM NaCl, 1 mM TCEP, pH:
Experiment: SAXS data collected at BM29, ESRF on 2021 Nov 21
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 2.2 nm
Dmax 9.5 nm
VolumePorod 56 nm3

SASDWY8 – β-Lactoglobulin A at 16.3 µM (pH 3.0)

Beta-lactoglobulin experimental SAS data
Beta-lactoglobulin Kratky plot
Sample: Beta-lactoglobulin , 20 kDa Bos taurus protein
Buffer: 20 mM citrate, 100 mM NaCl, 1 mM TCEP, pH:
Experiment: SAXS data collected at BM29, ESRF on 2021 Dec 3
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 2.2 nm
Dmax 7.3 nm
VolumePorod 55 nm3

SASDKZ8 – Mothers against decapentaplegic homolog 2, SMAD2, wild-type 0.74 mg/ml

Mothers against decapentaplegic homolog 2 experimental SAS data
Mothers against decapentaplegic homolog 2 Kratky plot
Sample: Mothers against decapentaplegic homolog 2 , 160 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2016 Nov 11
Conformational landscape of multidomain SMAD proteins Computational and Structural Biotechnology Journal (2021)
Gomes T, Martin-Malpartida P, Ruiz L, Aragón E, Cordeiro T, Macias M
RgGuinier 3.4 nm
Dmax 15.0 nm

SASDWZ8 – β-Lactoglobulin A at 19.6 μM (pH 3.0)

Beta-lactoglobulin experimental SAS data
Beta-lactoglobulin Kratky plot
Sample: Beta-lactoglobulin , 20 kDa Bos taurus protein
Buffer: 20 mM citrate, 100 mM NaCl, 1 mM TCEP, pH:
Experiment: SAXS data collected at BM29, ESRF on 2021 Dec 3
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 2.1 nm
Dmax 6.8 nm
VolumePorod 48 nm3

SASDK29 – Mothers against decapentaplegic homolog 2, SMAD2, wild-type 1.3 mg/ml

Mothers against decapentaplegic homolog 2 experimental SAS data
Mothers against decapentaplegic homolog 2 Kratky plot
Sample: Mothers against decapentaplegic homolog 2 , 160 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2016 Nov 11
Conformational landscape of multidomain SMAD proteins Computational and Structural Biotechnology Journal (2021)
Gomes T, Martin-Malpartida P, Ruiz L, Aragón E, Cordeiro T, Macias M
RgGuinier 3.8 nm
Dmax 21.0 nm

SASDW29 – β-Lactoglobulin A at 27.2 μM (pH 3.0)

Beta-lactoglobulin experimental SAS data
Beta-lactoglobulin Kratky plot
Sample: Beta-lactoglobulin , 20 kDa Bos taurus protein
Buffer: 20 mM citrate, 100 mM NaCl, 1 mM TCEP, pH:
Experiment: SAXS data collected at BM29, ESRF on 2021 Dec 3
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 2.2 nm
Dmax 8.5 nm
VolumePorod 57 nm3

SASDK39 – Mothers against decapentaplegic homolog 2, SMAD2, wild-type 2.5 mg/ml

Mothers against decapentaplegic homolog 2 experimental SAS data
Mothers against decapentaplegic homolog 2 Kratky plot
Sample: Mothers against decapentaplegic homolog 2 , 160 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2016 Nov 11
Conformational landscape of multidomain SMAD proteins Computational and Structural Biotechnology Journal (2021)
Gomes T, Martin-Malpartida P, Ruiz L, Aragón E, Cordeiro T, Macias M
RgGuinier 3.8 nm
Dmax 20.0 nm

SASDW39 – β-Lactoglobulin A at 28.8 μM (pH 3.0)

Beta-lactoglobulin experimental SAS data
Beta-lactoglobulin Kratky plot
Sample: Beta-lactoglobulin , 20 kDa Bos taurus protein
Buffer: 20 mM citrate, 100 mM NaCl, 1 mM TCEP, pH:
Experiment: SAXS data collected at BM29, ESRF on 2021 Dec 3
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 2.2 nm
Dmax 7.2 nm
VolumePorod 47 nm3

SASDK49 – Mothers against decapentaplegic homolog 2, SMAD2, wild-type 3mg/ml

Mothers against decapentaplegic homolog 2 experimental SAS data
Mothers against decapentaplegic homolog 2 Kratky plot
Sample: Mothers against decapentaplegic homolog 2 , 160 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2016 Nov 11
Conformational landscape of multidomain SMAD proteins Computational and Structural Biotechnology Journal (2021)
Gomes T, Martin-Malpartida P, Ruiz L, Aragón E, Cordeiro T, Macias M
RgGuinier 4.3 nm
Dmax 23.0 nm

SASDW49 – β-Lactoglobulin A at 38 μM (pH 3.0)

Beta-lactoglobulin experimental SAS data
Beta-lactoglobulin Kratky plot
Sample: Beta-lactoglobulin , 20 kDa Bos taurus protein
Buffer: 20 mM citrate, 100 mM NaCl, 1 mM TCEP, pH:
Experiment: SAXS data collected at BM29, ESRF on 2021 Dec 3
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 2.2 nm
Dmax 8.0 nm
VolumePorod 60 nm3

SASDK59 – Mothers against decapentaplegic homolog 2, SMAD2, linker fragment (amino acids 175-262)

Mothers against decapentaplegic homolog 2 (linker) experimental SAS data
Mothers against decapentaplegic homolog 2 (linker) Kratky plot
Sample: Mothers against decapentaplegic homolog 2 (linker) monomer, 10 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2016 Nov 11
Conformational landscape of multidomain SMAD proteins Computational and Structural Biotechnology Journal (2021)
Gomes T, Martin-Malpartida P, Ruiz L, Aragón E, Cordeiro T, Macias M
RgGuinier 2.9 nm
Dmax 14.0 nm
VolumePorod 20 nm3

SASDW59 – β-Lactoglobulin A at 58.2 μM (pH 3.0)

Beta-lactoglobulin experimental SAS data
Beta-lactoglobulin Kratky plot
Sample: Beta-lactoglobulin , 20 kDa Bos taurus protein
Buffer: 20 mM citrate, 100 mM NaCl, 1 mM TCEP, pH:
Experiment: SAXS data collected at BM29, ESRF on 2021 Dec 3
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 2.2 nm
Dmax 7.5 nm
VolumePorod 53 nm3

SASDK69 – Mothers against decapentaplegic homolog 2, SMAD2, linker-MH2 fragment (amino acids 186-467) 0.5 mg/ml

Mothers against decapentaplegic homolog 2 (linker-MH2) experimental SAS data
Mothers against decapentaplegic homolog 2 (linker-MH2) Kratky plot
Sample: Mothers against decapentaplegic homolog 2 (linker-MH2) , 99 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2016 Nov 11
Conformational landscape of multidomain SMAD proteins Computational and Structural Biotechnology Journal (2021)
Gomes T, Martin-Malpartida P, Ruiz L, Aragón E, Cordeiro T, Macias M
RgGuinier 3.6 nm
Dmax 15.0 nm

SASDW69 – β-Lactoglobulin A at 87.5 μM (pH 3.0)

Beta-lactoglobulin experimental SAS data
Beta-lactoglobulin Kratky plot
Sample: Beta-lactoglobulin , 20 kDa Bos taurus protein
Buffer: 20 mM citrate, 100 mM NaCl, 1 mM TCEP, pH:
Experiment: SAXS data collected at BM29, ESRF on 2021 Dec 3
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 2.2 nm
Dmax 7.5 nm
VolumePorod 53 nm3

SASDK79 – Mothers against decapentaplegic homolog 2, SMAD2, linker-MH2 fragment (amino acids 186-467) 1.1 mg/ml

Mothers against decapentaplegic homolog 2 (linker-MH2) experimental SAS data
Mothers against decapentaplegic homolog 2 (linker-MH2) Kratky plot
Sample: Mothers against decapentaplegic homolog 2 (linker-MH2) , 99 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2016 Nov 11
Conformational landscape of multidomain SMAD proteins Computational and Structural Biotechnology Journal (2021)
Gomes T, Martin-Malpartida P, Ruiz L, Aragón E, Cordeiro T, Macias M
RgGuinier 3.7 nm
Dmax 17.0 nm

SASDW79 – β-Lactoglobulin A at 116.3 μM (pH 3.0)

Beta-lactoglobulin experimental SAS data
Beta-lactoglobulin Kratky plot
Sample: Beta-lactoglobulin , 20 kDa Bos taurus protein
Buffer: 20 mM citrate, 100 mM NaCl, 1 mM TCEP, pH:
Experiment: SAXS data collected at BM29, ESRF on 2021 Dec 3
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 2.2 nm
Dmax 8.5 nm
VolumePorod 51 nm3

SASDK89 – Mothers against decapentaplegic homolog 2, SMAD2, linker-MH2 fragment (amino acids 186-467) 2.2 mg/ml

Mothers against decapentaplegic homolog 2 (linker-MH2) experimental SAS data
Mothers against decapentaplegic homolog 2 (linker-MH2) Kratky plot
Sample: Mothers against decapentaplegic homolog 2 (linker-MH2) , 99 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2016 Nov 11
Conformational landscape of multidomain SMAD proteins Computational and Structural Biotechnology Journal (2021)
Gomes T, Martin-Malpartida P, Ruiz L, Aragón E, Cordeiro T, Macias M
RgGuinier 4.2 nm
Dmax 19.0 nm

SASDW89 – Proliferating Cell Nuclear Antigen (PCNA) sliding clamp

Proliferating cell nuclear antigen experimental SAS data
Proliferating cell nuclear antigen Kratky plot
Sample: Proliferating cell nuclear antigen trimer, 87 kDa Homo sapiens protein
Buffer: 137 mM NaCl, 2.7 mM KCl, 10 mM sodium phosphate, 2 mM potassium phosphate (PBS), pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2012 Apr 23
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 3.4 nm
Dmax 9.0 nm
VolumePorod 137 nm3

SASDK99 – Mothers against decapentaplegic homolog 2, SMAD2, C-terminus deletion (Δ461-467) 1 mg/ml

Mothers against decapentaplegic homolog 2 (C-terminus deletion) experimental SAS data
Mothers against decapentaplegic homolog 2 (C-terminus deletion) Kratky plot
Sample: Mothers against decapentaplegic homolog 2 (C-terminus deletion) , 158 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2016 Nov 11
Conformational landscape of multidomain SMAD proteins Computational and Structural Biotechnology Journal (2021)
Gomes T, Martin-Malpartida P, Ruiz L, Aragón E, Cordeiro T, Macias M
RgGuinier 4.1 nm
Dmax 17.0 nm

SASDW99 – Proliferating cell nuclear antigen:PCNA-associated factor (PCNA:P15) titration, 150 µM:30 µM

Proliferating cell nuclear antigenPCNA-associated factor experimental SAS data
Proliferating cell nuclear antigen PCNA-associated factor Kratky plot
Sample: Proliferating cell nuclear antigen trimer, 87 kDa Homo sapiens protein
PCNA-associated factor monomer, 12 kDa Homo sapiens protein
Buffer: 137 mM NaCl, 2.7 mM KCl, 10 mM sodium phosphate, 2 mM potassium phosphate (PBS), pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2012 Apr 23
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 3.5 nm
Dmax 9.7 nm
VolumePorod 128 nm3

SASDKA9 – Mothers against decapentaplegic homolog 2, SMAD2, C-terminus deletion (Δ461-467) 2 mg/ml

Mothers against decapentaplegic homolog 2 (C-terminus deletion) experimental SAS data
Mothers against decapentaplegic homolog 2 (C-terminus deletion) Kratky plot
Sample: Mothers against decapentaplegic homolog 2 (C-terminus deletion) , 158 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2016 Nov 11
Conformational landscape of multidomain SMAD proteins Computational and Structural Biotechnology Journal (2021)
Gomes T, Martin-Malpartida P, Ruiz L, Aragón E, Cordeiro T, Macias M
RgGuinier 4.3 nm
Dmax 20.0 nm

SASDWA9 – Proliferating cell nuclear antigen:PCNA-associated factor (PCNA:P15) titration, 150 µM:60 µM

Proliferating cell nuclear antigenPCNA-associated factor experimental SAS data
Proliferating cell nuclear antigen PCNA-associated factor Kratky plot
Sample: Proliferating cell nuclear antigen trimer, 87 kDa Homo sapiens protein
PCNA-associated factor monomer, 12 kDa Homo sapiens protein
Buffer: 137 mM NaCl, 2.7 mM KCl, 10 mM sodium phosphate, 2 mM potassium phosphate (PBS), pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2012 Apr 23
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 3.5 nm
Dmax 10.0 nm
VolumePorod 158 nm3

SASDKB9 – Mothers against decapentaplegic homolog 2, SMAD2, C-terminus deletion (Δ461-467) 3.8 mg/ml

Mothers against decapentaplegic homolog 2 (C-terminus deletion) experimental SAS data
Mothers against decapentaplegic homolog 2 (C-terminus deletion) Kratky plot
Sample: Mothers against decapentaplegic homolog 2 (C-terminus deletion) , 158 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2016 Nov 11
Conformational landscape of multidomain SMAD proteins Computational and Structural Biotechnology Journal (2021)
Gomes T, Martin-Malpartida P, Ruiz L, Aragón E, Cordeiro T, Macias M
RgGuinier 4.6 nm
Dmax 22.0 nm

SASDWB9 – Proliferating cell nuclear antigen:PCNA-associated factor (PCNA:P15) titration, 150 µM:90 µM

Proliferating cell nuclear antigenPCNA-associated factor experimental SAS data
Proliferating cell nuclear antigen PCNA-associated factor Kratky plot
Sample: Proliferating cell nuclear antigen trimer, 87 kDa Homo sapiens protein
PCNA-associated factor monomer, 12 kDa Homo sapiens protein
Buffer: 137 mM NaCl, 2.7 mM KCl, 10 mM sodium phosphate, 2 mM potassium phosphate (PBS), pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2012 Apr 23
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 3.7 nm
Dmax 11.0 nm
VolumePorod 184 nm3

SASDKC9 – Mothers against decapentaplegic homolog 4, SMAD4, wild-type

Mothers against decapentaplegic homolog 4 experimental SAS data
Mothers against decapentaplegic homolog 4 Kratky plot
Sample: Mothers against decapentaplegic homolog 4 monomer, 60 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2015 Nov 4
Conformational landscape of multidomain SMAD proteins Computational and Structural Biotechnology Journal (2021)
Gomes T, Martin-Malpartida P, Ruiz L, Aragón E, Cordeiro T, Macias M
RgGuinier 4.4 nm
Dmax 22.0 nm

SASDWC9 – Proliferating cell nuclear antigen:PCNA-associated factor (PCNA:P15) titration, 150 µM:150 µM

Proliferating cell nuclear antigenPCNA-associated factor experimental SAS data
Proliferating cell nuclear antigen PCNA-associated factor Kratky plot
Sample: Proliferating cell nuclear antigen trimer, 87 kDa Homo sapiens protein
PCNA-associated factor monomer, 12 kDa Homo sapiens protein
Buffer: 137 mM NaCl, 2.7 mM KCl, 10 mM sodium phosphate, 2 mM potassium phosphate (PBS), pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2012 Apr 23
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 3.7 nm
Dmax 11.0 nm
VolumePorod 219 nm3

SASDKD9 – Mothers against decapentaplegic homolog 4, SMAD4, linker fragment (amino acids 141-271)

Mothers against decapentaplegic homolog 4 (linker) experimental SAS data
Mothers against decapentaplegic homolog 4 (linker) Kratky plot
Sample: Mothers against decapentaplegic homolog 4 (linker) monomer, 14 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2015 Apr 20
Conformational landscape of multidomain SMAD proteins Computational and Structural Biotechnology Journal (2021)
Gomes T, Martin-Malpartida P, Ruiz L, Aragón E, Cordeiro T, Macias M
RgGuinier 3.7 nm
Dmax 17.5 nm
VolumePorod 45 nm3

SASDWD9 – Proliferating cell nuclear antigen:PCNA-associated factor (PCNA:P15) titration, 150 µM:200 µM

Proliferating cell nuclear antigenPCNA-associated factor experimental SAS data
Proliferating cell nuclear antigen PCNA-associated factor Kratky plot
Sample: Proliferating cell nuclear antigen trimer, 87 kDa Homo sapiens protein
PCNA-associated factor monomer, 12 kDa Homo sapiens protein
Buffer: 137 mM NaCl, 2.7 mM KCl, 10 mM sodium phosphate, 2 mM potassium phosphate (PBS), pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2012 Apr 23
KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models Journal of Molecular Biology :169103 (2025)
Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T
RgGuinier 3.7 nm
Dmax 11.0 nm
VolumePorod 208 nm3

SASDKE9 – Mothers against decapentaplegic homolog 4, SMAD4, linker-MH2 fragment (amino acids 150-552)

Mothers against decapentaplegic homolog 4 (linker-MH2) experimental SAS data
Mothers against decapentaplegic homolog 4 (linker-MH2) Kratky plot
Sample: Mothers against decapentaplegic homolog 4 (linker-MH2) monomer, 44 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BM29, ESRF on 2015 Apr 20
Conformational landscape of multidomain SMAD proteins Computational and Structural Biotechnology Journal (2021)
Gomes T, Martin-Malpartida P, Ruiz L, Aragón E, Cordeiro T, Macias M
RgGuinier 3.3 nm
Dmax 17.0 nm
VolumePorod 80 nm3

SASDLE9 – Suppressor of Copper Sensitivity C protein from Caulobacter crescentus

Thioredoxin domain-containing protein experimental SAS data
Suppressor of Copper Sensitivity C protein from Caulobacter crescentus Rg histogram
Sample: Thioredoxin domain-containing protein trimer, 73 kDa Caulobacter vibrioides (strain … protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Aug 21
The suppressor of copper sensitivity protein C from Caulobacter crescentus is a trimeric disulfide isomerase that binds copper(I) with subpicomolar affinity Acta Crystallographica Section D Structural Biology 78(3):337-352 (2022)
Petit G, Hong Y, Djoko K, Whitten A, Furlong E, McCoy A, Gulbis J, Totsika M, Martin J, Halili M
RgGuinier 3.9 nm
Dmax 12.0 nm
VolumePorod 97 nm3