SASBDB entries for UniProt ID:

SASDXW4 – EGFR kinase domain duplication mutant (KDD) at 2.7 mg/ml

UniProt ID: Q504U8 (651-993) Receptor protein-tyrosine kinase (duplication mutant)
Receptor protein-tyrosine kinase (duplication mutant) experimental SAS data
Receptor protein-tyrosine kinase (duplication mutant) Kratky plot
Sample: Receptor protein-tyrosine kinase (duplication mutant) monomer, 80 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 250 mM NaCl, 250 mM KCl, pH: 8
Experiment: SAXS data collected at Rigaku MicroMax-007HF, Yale University on 2022 Mar 22
The role of kinase domain dimerization in EGFR activation
Zaritza Petrova
RgGuinier 4.5 nm
Dmax 14.9 nm
VolumePorod 190 nm3

SASDXX4 – Serratia marcescens poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB

UniProt ID: A0A2V4FWX5 (18-668) Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB
Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB experimental SAS data
ALPHAFOLD model
Sample: Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB monomer, 73 kDa Serratia marcescens protein
Buffer: phosphate-buffered saline, pH: 7.4
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2025 Feb 3
Structural, biophysical and biochemical studies of CAZYmes involved in exopolysaccharides degradation of microbial biofilms Universidade de São Paulo Master's thesis (2025)
Amanda Freitas Cruz
RgGuinier 2.9 nm
Dmax 9.4 nm
VolumePorod 102 nm3

SASDXY4 – Serratia marcescens truncated Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB

UniProt ID: A0A2V4FWX5 (40-653) Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB
Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB experimental SAS data
ALPHAFOLD model
Sample: Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB monomer, 69 kDa Serratia marcescens protein
Buffer: phosphate-buffered saline, pH: 7.4
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2025 Feb 3
Structural, biophysical and biochemical studies of CAZYmes involved in exopolysaccharides degradation of microbial biofilms Universidade de São Paulo Master's thesis (2025)
Amanda Freitas Cruz
RgGuinier 2.8 nm
Dmax 9.0 nm
VolumePorod 102 nm3

SASDXZ4 – Hemolysin A Type 1 Secretion System (Hly T1SS)

UniProt ID: Q1R2T6 (2-707) Alpha-hemolysin translocation ATP-binding protein HlyB

UniProt ID: A0A236M9V9 (1-1024) HlyA (GFP-Hemolysin with Flag-Tag insertion)

UniProt ID: Q1R2T7 (1-478) Membrane fusion protein (MFP) family protein (R14C; L229V)

UniProt ID: P02930 (1-493) Outer membrane protein TolC
Alpha-hemolysin translocation ATP-binding protein HlyBHlyA (GFP-Hemolysin with Flag-Tag insertion)Membrane fusion protein (MFP) family protein (R14C; L229V)Outer membrane protein TolC experimental SAS data
DAMMIF model
Sample: Alpha-hemolysin translocation ATP-binding protein HlyB hexamer, 480 kDa Escherichia coli (strain … protein
HlyA (GFP-Hemolysin with Flag-Tag insertion) monomer, 144 kDa Escherichia coli protein
Membrane fusion protein (MFP) family protein (R14C; L229V) hexamer, 327 kDa Escherichia coli (strain … protein
Outer membrane protein TolC trimer, 161 kDa Escherichia coli (strain … protein
Buffer: 50 mM Tris, 150 mM NaCl, 10 mM CaCl2, 0.0063% glyco-diosgenin (GDN), pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2023 Jun 29
Molecular Insights into CLD Domain Dynamics and Toxin Recruitment of the HlyA E. coli T1SS Journal of Molecular Biology :169485 (2025)
Gentile R, Schott-Verdugo S, Khosa S, Günes C, Bonus M, Reiners J, Smits S, Schmitt L, Gohlke H
RgGuinier 11.4 nm
Dmax 46.2 nm
VolumePorod 2837 nm3

SASDX45 – IgA protease (ThomasA) 31-1167

UniProt ID: Q9AES2 (31-1167) IgA protease
IgA protease experimental SAS data
IgA protease Kratky plot
Sample: IgA protease monomer, 127 kDa Thomasclavelia ramosa protein
Buffer: 50 mM Tris-HCl pH 7.5, 100 mM NaCl, 2% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Apr 19
Molecular basis of Fab-dependent IgA antibody recognition by gut-bacterial metallopeptidases The EMBO Journal (2025)
Márquez-Moñino M, Martínez Gascueña A, Azzam T, Persson A, Manzanares-Gomez A, Aguillo-Urarte M, Brown T, Montero-Sagarminaga A, Lood R, Naegeli A, Connell S, Sastre D, Sundberg E, Trastoy B
RgGuinier 6.4 nm
Dmax 25.0 nm
VolumePorod 208 nm3

SASDX55 – IgA protease (ThomasA) 31-878

UniProt ID: Q9AES2 (31-878) IgA protease
IgA protease experimental SAS data
IgA protease Kratky plot
Sample: IgA protease monomer, 96 kDa Thomasclavelia ramosa protein
Buffer: 50 mM Tris-HCl pH 7.5, 100 mM NaCl, 2% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Apr 19
Molecular basis of Fab-dependent IgA antibody recognition by gut-bacterial metallopeptidases The EMBO Journal (2025)
Márquez-Moñino M, Martínez Gascueña A, Azzam T, Persson A, Manzanares-Gomez A, Aguillo-Urarte M, Brown T, Montero-Sagarminaga A, Lood R, Naegeli A, Connell S, Sastre D, Sundberg E, Trastoy B
RgGuinier 3.4 nm
Dmax 10.6 nm
VolumePorod 101 nm3

SASDX65 – IgA protease (ThomasA) 323-878

UniProt ID: Q9AES2 (323-878) IgA protease
IgA protease experimental SAS data
IgA protease Kratky plot
Sample: IgA protease monomer, 64 kDa Thomasclavelia ramosa protein
Buffer: 50 mM Tris-HCl pH 7.5, 100 mM NaCl, 2% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Apr 19
Molecular basis of Fab-dependent IgA antibody recognition by gut-bacterial metallopeptidases The EMBO Journal (2025)
Márquez-Moñino M, Martínez Gascueña A, Azzam T, Persson A, Manzanares-Gomez A, Aguillo-Urarte M, Brown T, Montero-Sagarminaga A, Lood R, Naegeli A, Connell S, Sastre D, Sundberg E, Trastoy B
RgGuinier 3.0 nm
Dmax 9.2 nm
VolumePorod 72 nm3

SASDX75 – Virulence factor family protein (VirJD1) from Brucella abortus

UniProt ID: A0AAE9RTQ7 (43-265) Virulence factor family protein
Virulence factor family protein experimental SAS data
Virulence factor family protein Kratky plot
Sample: Virulence factor family protein monomer, 24 kDa Brucella abortus protein
Buffer: 50 mM Tris pH 8.0, 200 mM NaCl, 5% v/v glycerol, pH:
Experiment: SAXS data collected at SWING, SOLEIL on 2023 Jul 12
Crystal structure of the virulence protein J (VirJ) domain 1 from Brucella abortus. Acta Crystallogr F Struct Biol Commun (2025)
Dugelay C, Ferrarin S, Terradot L
RgGuinier 1.8 nm
Dmax 6.1 nm
VolumePorod 39 nm3

SASDX95 – DNA repair protein RAD51 homolog 1 (RAD51) [F86E, A89E] in complex with Breast cancer type 2 susceptibility protein (BRCA2) truncation containing the second, third and fourth BRC repeats (BRC2-4) at 1 mg/mL

UniProt ID: P51587 (1212-1551) Breast cancer type 2 susceptibility protein (BRC repeats 2-4)

UniProt ID: Q06609 (1-339) DNA repair protein RAD51 homolog 1 (F86E A89E)
Breast cancer type 2 susceptibility protein (BRC repeats 2-4)DNA repair protein RAD51 homolog 1 (F86E A89E) experimental SAS data
Breast cancer type 2 susceptibility protein (BRC repeats 2-4) DNA repair protein RAD51 homolog 1 (F86E A89E) Kratky plot
Sample: Breast cancer type 2 susceptibility protein (BRC repeats 2-4) monomer, 39 kDa Homo sapiens protein
DNA repair protein RAD51 homolog 1 (F86E A89E) trimer, 111 kDa Homo sapiens protein
Buffer: 20 mM K₂HPO₄/KH₂PO₄, 100 mM NaCl, 200 mM Li₂SO₄, 5% glycerol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Dec 2
Breaking new ground into RAD51–BRC repeats interplay in Homologous Recombination (2025)
Rinaldi F, Franco P, Veronesi M, Romeo E, Bresciani V, Varignani G, Catalano F, Bernetti M, Masetti M, Langer J, Girotto S, Cavalli A
RgGuinier 6.5 nm
Dmax 28.5 nm
VolumePorod 334 nm3

SASDXA5 – DNA repair protein RAD51 homolog 1 (RAD51) [F86E, A89E] in complex with Breast cancer type 2 susceptibility protein (BRCA2) truncation containing the second, third and fourth BRC repeats (BRC2-4) at 2 mg/mL

UniProt ID: P51587 (1212-1551) Breast cancer type 2 susceptibility protein (BRC repeats 2-4)

UniProt ID: Q06609 (1-339) DNA repair protein RAD51 homolog 1 (F86E A89E)
Breast cancer type 2 susceptibility protein (BRC repeats 2-4)DNA repair protein RAD51 homolog 1 (F86E A89E) experimental SAS data
Breast cancer type 2 susceptibility protein (BRC repeats 2-4) DNA repair protein RAD51 homolog 1 (F86E A89E) Kratky plot
Sample: Breast cancer type 2 susceptibility protein (BRC repeats 2-4) monomer, 39 kDa Homo sapiens protein
DNA repair protein RAD51 homolog 1 (F86E A89E) trimer, 111 kDa Homo sapiens protein
Buffer: 20 mM K₂HPO₄/KH₂PO₄, 100 mM NaCl, 200 mM Li₂SO₄, 5% glycerol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Dec 2
Breaking new ground into RAD51–BRC repeats interplay in Homologous Recombination (2025)
Rinaldi F, Franco P, Veronesi M, Romeo E, Bresciani V, Varignani G, Catalano F, Bernetti M, Masetti M, Langer J, Girotto S, Cavalli A
RgGuinier 6.5 nm
Dmax 28.5 nm
VolumePorod 473 nm3