SASBDB entries for UniProt ID:

SASDPU7 – Amyloid Beta 1-42 (cluster 1, Set 1, initial state)

UniProt ID: P05067 (672-713) Amyloid-beta precursor protein
Amyloid-beta precursor protein experimental SAS data
DAMMIN model
Sample: Amyloid-beta precursor protein, 5 kDa Homo sapiens protein
Buffer: 1 mM Hepes, 0.12 % NH4OH, pH: 10.7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Nov 2
Time-resolved small-angle X-ray scattering study of polymorphic nature of Aß42 oligomerisation
Tia Cheremnykh
RgGuinier 3.5 nm
Dmax 15.0 nm

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

UniProt ID: A0A2Y9UCL1 (None-None) Monooxygenase (M154I, A283T)
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

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

UniProt ID: A0A2Y9UCL1 (None-None) Monooxygenase (M154I, A283T)
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

SASDPX7 – DNA protection during starvation protein (Dps) loaded with FeSO4⋅7H2O in the amount corresponding to 50 iron atoms per dodecamer. Anomalous SAXS spanning the X-ray Fe-absorption edge 7.100-7.133 keV.

UniProt ID: P0ABT2 (1-167) DNA protection during starvation protein
DNA protection during starvation protein experimental SAS data
DAMMIN model
Sample: DNA protection during starvation protein dodecamer, 224 kDa Escherichia coli (strain … protein
Buffer: 50 mM NaCl, 0.5 mM EDTA, 50 mM Tris-HCl, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Oct 5
An Anomalous Small-Angle X-Ray Scattering Study of the Formation of Iron Clusters in the Inner Cavity of the Ferritin-Like Protein Dps Moscow University Physics Bulletin 77(6):858-867 (2023)
Gordienko A, Mozhaev A, Gibizova V, Dadinova L
RgGuinier 3.8 nm
Dmax 14.0 nm
VolumePorod 32 nm3

SASDPY7 – DNA protection during starvation protein (Dps) loaded with FeSO4⋅7H2O in the amount corresponding to 500 iron atoms per dodecamer. Anomalous SAXS spanning the X-ray Fe-absorption edge 7.100-7.133 keV.

UniProt ID: P0ABT2 (1-167) DNA protection during starvation protein
DNA protection during starvation protein experimental SAS data
DAMMIN model
Sample: DNA protection during starvation protein dodecamer, 224 kDa Escherichia coli (strain … protein
Buffer: 50 mM NaCl, 0.5 mM EDTA, 50 mM Tris-HCl, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Oct 5
An Anomalous Small-Angle X-Ray Scattering Study of the Formation of Iron Clusters in the Inner Cavity of the Ferritin-Like Protein Dps Moscow University Physics Bulletin 77(6):858-867 (2023)
Gordienko A, Mozhaev A, Gibizova V, Dadinova L
RgGuinier 7.4 nm
Dmax 12.0 nm

SASDPZ7 – DNA protection during starvation protein (Dps) loaded with FeSO4⋅7H2O in the amount corresponding to 2000 iron atoms per dodecamer. Anomalous SAXS spanning the X-ray Fe-absorption edge 7.100-7.133 keV.

UniProt ID: P0ABT2 (1-167) DNA protection during starvation protein
DNA protection during starvation protein experimental SAS data
DAMMIN model
Sample: DNA protection during starvation protein dodecamer, 224 kDa Escherichia coli (strain … protein
Buffer: 50 mM NaCl, 0.5 mM EDTA, 50 mM Tris-HCl, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Oct 5
An Anomalous Small-Angle X-Ray Scattering Study of the Formation of Iron Clusters in the Inner Cavity of the Ferritin-Like Protein Dps Moscow University Physics Bulletin 77(6):858-867 (2023)
Gordienko A, Mozhaev A, Gibizova V, Dadinova L
RgGuinier 7.1 nm
Dmax 14.0 nm

SASDP28 – Growth factor receptor-bound protein 2 (GRB2) - wild-type monomer

UniProt ID: P62993 (1-217) Growth factor receptor-bound protein 2
Growth factor receptor-bound protein 2 experimental SAS data
PYMOL model
Sample: Growth factor receptor-bound protein 2 monomer, 28 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Oct 31
GRB2 dimerization mediated by SH2 domain-swapping is critical for T cell signaling and cytokine production. Sci Rep 13(1):3505 (2023)
Sandouk A, Xu Z, Baruah S, Tremblay M, Hopkins JB, Chakravarthy S, Gakhar L, Schnicker NJ, Houtman JCD
RgGuinier 2.5 nm
Dmax 9.0 nm
VolumePorod 40 nm3

SASDP38 – Growth factor receptor-bound protein 2 (GRB2) - wild-type dimer

UniProt ID: P62993 (1-217) Growth factor receptor-bound protein 2
Growth factor receptor-bound protein 2 experimental SAS data
PYMOL model
Sample: Growth factor receptor-bound protein 2 dimer, 55 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Oct 31
GRB2 dimerization mediated by SH2 domain-swapping is critical for T cell signaling and cytokine production. Sci Rep 13(1):3505 (2023)
Sandouk A, Xu Z, Baruah S, Tremblay M, Hopkins JB, Chakravarthy S, Gakhar L, Schnicker NJ, Houtman JCD
RgGuinier 3.7 nm
Dmax 14.0 nm
VolumePorod 110 nm3

SASDP48 – Growth factor receptor-bound protein 2 (GRB2) - N188D/N214D mutant monomer

UniProt ID: P62993 (1-217) Growth factor receptor-bound protein 2 (N188D, N214D)
Growth factor receptor-bound protein 2 (N188D, N214D) experimental SAS data
PYMOL model
Sample: Growth factor receptor-bound protein 2 (N188D, N214D) monomer, 28 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Oct 31
GRB2 dimerization mediated by SH2 domain-swapping is critical for T cell signaling and cytokine production. Sci Rep 13(1):3505 (2023)
Sandouk A, Xu Z, Baruah S, Tremblay M, Hopkins JB, Chakravarthy S, Gakhar L, Schnicker NJ, Houtman JCD
RgGuinier 2.5 nm
Dmax 9.5 nm
VolumePorod 39 nm3

SASDP58 – Growth factor receptor-bound protein 2 (GRB2) - N188D/N214D mutant dimer

UniProt ID: P62993 (1-217) Growth factor receptor-bound protein 2 (N188D, N214D)
Growth factor receptor-bound protein 2 (N188D, N214D) experimental SAS data
PYMOL model
Sample: Growth factor receptor-bound protein 2 (N188D, N214D) dimer, 55 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Oct 31
GRB2 dimerization mediated by SH2 domain-swapping is critical for T cell signaling and cytokine production. Sci Rep 13(1):3505 (2023)
Sandouk A, Xu Z, Baruah S, Tremblay M, Hopkins JB, Chakravarthy S, Gakhar L, Schnicker NJ, Houtman JCD
RgGuinier 4.1 nm
Dmax 15.0 nm
VolumePorod 140 nm3