SASBDB entries for UniProt ID:

SASDKE4 – Polymorphic DNA protection during starvation protein (Dps)-DNA сo-сrystals

UniProt ID: P0ABT2 (None-None) DNA protection during starvation protein
DNA protection during starvation protein experimental SAS data
DNA protection during starvation protein Kratky plot
Sample: DNA protection during starvation protein dodecamer, 224 kDa Escherichia coli (strain … protein
Buffer: 10 mM Tris-HCl, 100 mM NaCl, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Oct 28
Polymorphic Protective Dps-DNA Co-Crystals by Cryo Electron Tomography and Small Angle X-Ray Scattering. Biomolecules 10(1) (2019)
Kamyshinsky R, Chesnokov Y, Dadinova L, Mozhaev A, Orlov I, Petoukhov M, Orekhov A, Shtykova E, Vasiliev A

SASDKF4 – DNA binding protein of starvation (DPS)

UniProt ID: A7ZJM7 (1-167) DNA protection during starvation protein
DNA protection during starvation protein experimental SAS data
DAMMIN model
Sample: DNA protection during starvation protein dodecamer, 225 kDa Escherichia coli protein
Buffer: 50 mM Tris-HCl, 50 mM NaCl, 0.5 mM EDTA, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Nov 26
Spatial Organization of Dps and DNA-Dps Complexes. J Mol Biol :166930 (2021)
Dubrovin EV, Dadinova LA, Petoukhov MV, Yu Soshinskaya E, Mozhaev AA, Klinov DV, Schäffer TE, Shtykova EV, Batishchev OV
RgGuinier 3.9 nm
Dmax 14.0 nm
VolumePorod 314 nm3

SASDKJ4 – SARS-CoV-2 nsp7 and nsp8

UniProt ID: P0DTC1 (3860-3942) Replicase polyprotein 1a - nsp7

UniProt ID: P0DTC1 (3943-4140) Replicase polyprotein 1a - nsp8
Replicase polyprotein 1a - nsp7Replicase polyprotein 1a - nsp8 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Replicase polyprotein 1a - nsp7, 18 kDa Severe acute respiratory … protein
Replicase polyprotein 1a - nsp8, 44 kDa Severe acute respiratory … protein
Buffer: 50 mM Tris, pH 8.0, 100 mM NaCl, 4 mM DTT, 4 mM MgCl2, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Jun 19
Hallmarks of Alpha- and Betacoronavirus non-structural protein 7+8 complexes Science Advances 7(10):eabf1004 (2021)
Krichel B, Bylapudi G, Schmidt C, Blanchet C, Schubert R, Brings L, Koehler M, Zenobi R, Svergun D, Lorenzen K, Madhugiri R, Ziebuhr J, Uetrecht C
RgGuinier 3.4 nm
Dmax 13.5 nm
VolumePorod 92 nm3

SASDKL4 – High temperature requirement of human mitochondrial serine protease HTRA2 (S306A mutant; 10 mg/ml)

UniProt ID: O43464 (134-458) Serine protease HTRA2, mitochondrial
Serine protease HTRA2, mitochondrial experimental SAS data
SASREF MX model
Sample: Serine protease HTRA2, mitochondrial hexamer, 210 kDa Homo sapiens protein
Buffer: 20 mM HEPES-NaOH (pH 7.4), 120 mM NaCl, 1 mM EDTA, and 2% glycerol, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Jul 1
Oligomeric assembly regulating mitochondrial HtrA2 function as examined by methyl-TROSY NMR Proceedings of the National Academy of Sciences 118(11):e2025022118 (2021)
Toyama Y, Harkness R, Lee T, Maynes J, Kay L
RgGuinier 4.2 nm
Dmax 16.0 nm
VolumePorod 250 nm3

SASDKM4 – High temperature requirement of human mitochondrial serine protease HTRA2 (S306A mutant; 5 mg/ml)

UniProt ID: O43464 (134-458) Serine protease HTRA2, mitochondrial
Serine protease HTRA2, mitochondrial experimental SAS data
SASREF MX model
Sample: Serine protease HTRA2, mitochondrial hexamer, 210 kDa Homo sapiens protein
Buffer: 20 mM HEPES-NaOH (pH 7.4), 120 mM NaCl, 1 mM EDTA, and 2% glycerol, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Jul 1
Oligomeric assembly regulating mitochondrial HtrA2 function as examined by methyl-TROSY NMR Proceedings of the National Academy of Sciences 118(11):e2025022118 (2021)
Toyama Y, Harkness R, Lee T, Maynes J, Kay L
RgGuinier 3.8 nm
Dmax 15.0 nm
VolumePorod 213 nm3

SASDKN4 – High temperature requirement of human mitochondrial serine protease HTRA2 (S306A mutant; 2 mg/ml)

UniProt ID: O43464 (134-458) Serine protease HTRA2, mitochondrial
Serine protease HTRA2, mitochondrial experimental SAS data
SASREF MX model
Sample: Serine protease HTRA2, mitochondrial hexamer, 210 kDa Homo sapiens protein
Buffer: 20 mM HEPES-NaOH (pH 7.4), 120 mM NaCl, 1 mM EDTA, and 2% glycerol, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Jul 1
Oligomeric assembly regulating mitochondrial HtrA2 function as examined by methyl-TROSY NMR Proceedings of the National Academy of Sciences 118(11):e2025022118 (2021)
Toyama Y, Harkness R, Lee T, Maynes J, Kay L
RgGuinier 3.6 nm
Dmax 12.8 nm
VolumePorod 203 nm3

SASDKP4 – High temperature requirement of human mitochondrial serine protease HTRA2 (S306A mutant; 1 mg/ml)

UniProt ID: O43464 (134-458) Serine protease HTRA2, mitochondrial
Serine protease HTRA2, mitochondrial experimental SAS data
SASREF MX model
Sample: Serine protease HTRA2, mitochondrial hexamer, 210 kDa Homo sapiens protein
Buffer: 20 mM HEPES-NaOH (pH 7.4), 120 mM NaCl, 1 mM EDTA, and 2% glycerol, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Jul 1
Oligomeric assembly regulating mitochondrial HtrA2 function as examined by methyl-TROSY NMR Proceedings of the National Academy of Sciences 118(11):e2025022118 (2021)
Toyama Y, Harkness R, Lee T, Maynes J, Kay L
RgGuinier 3.4 nm
Dmax 12.0 nm
VolumePorod 168 nm3

SASDKQ4 – EspK secretion protein - full length

UniProt ID: P9WJC1 (484-729) ESX-1 secretion-associated protein EspK
ESX-1 secretion-associated protein EspK experimental SAS data
CORAL model
Sample: ESX-1 secretion-associated protein EspK monomer, 27 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 20 mM Tris-HCl pH, 300 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Sep 20
Structural Analysis of the Partially Disordered Protein EspK from Mycobacterium Tuberculosis Crystals 11(1):18 (2020)
Gijsbers A, Sánchez-Puig N, Gao Y, Peters P, Ravelli R, Siliqi D
RgGuinier 7.2 nm
Dmax 3.3 nm
VolumePorod 330 nm3

SASDKR4 – EspK secretion protein - C-terminal domain

UniProt ID: P9WJC1 (517-729) ESX-1 secretion-associated protein EspK
ESX-1 secretion-associated protein EspK experimental SAS data
GASBOR model
Sample: ESX-1 secretion-associated protein EspK monomer, 30 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 20 mM Tris-HCl pH, 300 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Apr 12
Structural Analysis of the Partially Disordered Protein EspK from Mycobacterium Tuberculosis Crystals 11(1):18 (2020)
Gijsbers A, Sánchez-Puig N, Gao Y, Peters P, Ravelli R, Siliqi D
RgGuinier 2.2 nm
Dmax 8.4 nm
VolumePorod 52 nm3

SASDKS4 – Teneurin-4 dimer wildtype in SEC buffer (20 mM HEPES, 150 mM NaCl)

UniProt ID: Q6N022 (373-2769) Teneurin-4
Teneurin-4 experimental SAS data
Teneurin-4 dimer wildtype in SEC buffer (20 mM HEPES, 150 mM NaCl) Rg histogram
Sample: Teneurin-4 dimer, 537 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.8
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 16
Teneurin4 dimer structures reveal a calcium‐stabilized compact conformation supporting homomeric trans‐interactions The EMBO Journal (2022)
Meijer D, Frias C, Beugelink J, Deurloo Y, Janssen B
RgGuinier 7.8 nm
Dmax 32.0 nm
VolumePorod 1280 nm3