SASBDB entries for UniProt ID:

SASDF23 – Cell wall synthesis protein Wag31(T73A) polymer (SEC-frames 320-324)

UniProt ID: P9WMU1 (None-None) Cell wall synthesis protein Wag31
Cell wall synthesis protein Wag31 experimental SAS data
Cell wall synthesis protein Wag31 Kratky plot
Sample: Cell wall synthesis protein Wag31, 30 kDa Mycobacterium tuberculosis protein
Buffer: 50mM Tris pH7.5, 300mM NaCl, 10% Glycerol, 1mM EDTA (ethylene diamine tetra acetic acid), 5mM β-mercaptoethanol (BME), pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2018 Jan 29
Higher order assembling of the mycobacterial polar growth factor DivIVA/Wag31. J Struct Biol :107429 (2019)
Choukate K, Gupta A, Basu B, Virk K, Ganguli M, Chaudhuri B
RgGuinier 10.2 nm

SASDF33 – Antigen 43/Fragment antigen-binding region Fab10C12 complex (Ag43-Fab)

UniProt ID: None (53-551) Alpha domain of Ag43a

UniProt ID: None (None-None) Fragment antigen-binding region Fab10C12
Alpha domain of Ag43aFragment antigen-binding region Fab10C12 experimental SAS data
DAMFILT model
Sample: Alpha domain of Ag43a monomer, 49 kDa Escherichia coli protein
Fragment antigen-binding region Fab10C12 monomer, 47 kDa Mus musculus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2016 Nov 3
Inhibition of aggregation and biofilm formation by Uropathogenic Escherichia coli
Andrew Whitten
RgGuinier 4.3 nm
Dmax 15.0 nm
VolumePorod 103 nm3

SASDF53 – Bruton's Tyrosine Kinase - kinase domain

UniProt ID: Q06187 (391-659) Bruton's tyrosine kinase, kinase domain
Bruton's tyrosine kinase, kinase domain experimental SAS data
DAMMIN model
Sample: Bruton's tyrosine kinase, kinase domain monomer, 32 kDa Homo sapiens protein
Buffer: 20mM Tris, 150mM NaCl, 1mM TCEP, 5% glycerol, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 May 11
Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms Nature Communications 11(1) (2020)
Duarte D, Lamontanara A, La Sala G, Jeong S, Sohn Y, Panjkovich A, Georgeon S, Kükenshöner T, Marcaida M, Pojer F, De Vivo M, Svergun D, Kim H, Dal Peraro M, Hantschel O
RgGuinier 2.1 nm
Dmax 6.8 nm
VolumePorod 52 nm3

SASDF73 – Bruton's Tyrosine Kinase - SH3-SH2-kinase domain

UniProt ID: Q06187 (214-659) Bruton's tyrosine kinase - Src homology 3-2 kinase domain
Bruton's tyrosine kinase - Src homology 3-2 kinase domain experimental SAS data
Bruton's Tyrosine Kinase - SH3-SH2-kinase domain Rg histogram
Sample: Bruton's tyrosine kinase - Src homology 3-2 kinase domain monomer, 52 kDa Homo sapiens protein
Buffer: 20mM Tris, 150mM NaCl, 1mM TCEP, 5% glycerol, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Nov 2
Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms Nature Communications 11(1) (2020)
Duarte D, Lamontanara A, La Sala G, Jeong S, Sohn Y, Panjkovich A, Georgeon S, Kükenshöner T, Marcaida M, Pojer F, De Vivo M, Svergun D, Kim H, Dal Peraro M, Hantschel O
RgGuinier 2.6 nm
Dmax 8.3 nm
VolumePorod 72 nm3

SASDF83 – Bruton's Tyrosine Kinase - Full-length

UniProt ID: Q06187 (1-659) Bruton's tyrosine kinase - full length
Bruton's tyrosine kinase - full length experimental SAS data
Bruton's Tyrosine Kinase - Full-length Rg histogram
Sample: Bruton's tyrosine kinase - full length monomer, 77 kDa Homo sapiens protein
Buffer: 20mM Tris, 150mM NaCl, 1mM TCEP, 5% glycerol, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Nov 3
Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms Nature Communications 11(1) (2020)
Duarte D, Lamontanara A, La Sala G, Jeong S, Sohn Y, Panjkovich A, Georgeon S, Kükenshöner T, Marcaida M, Pojer F, De Vivo M, Svergun D, Kim H, Dal Peraro M, Hantschel O
RgGuinier 4.0 nm
Dmax 15.6 nm
VolumePorod 114 nm3

SASDF93 – Ignicoccus islandicus malate dehydrogenase

UniProt ID: A0A0U3FQH7 (None-None) Malate dehydrogenase
Malate dehydrogenase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Malate dehydrogenase tetramer, 134 kDa Ignicoccus islandicus DSM … protein
Buffer: 50 mM Tris-HCl 50 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 5
The archaeal LDH-like malate dehydrogenase from Ignicoccus islandicus displays dual substrate recognition, hidden allostery and a non-canonical tetrameric oligomeric organization Journal of Structural Biology (2019)
Roche J, Girard E, Mas C, Madern D
RgGuinier 3.3 nm
Dmax 9.0 nm
VolumePorod 198 nm3

SASDFA3 – Human ATP-citrate synthase (ACLY) full length in HBS

UniProt ID: P53396-1 (None-None) ATP-citrate synthase
ATP-citrate synthase experimental SAS data
ATP-citrate synthase Kratky plot
Sample: ATP-citrate synthase tetramer, 458 kDa Homo sapiens protein
Buffer: 20mM HEPES, 150mM NaCl, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 4
Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle. Nature 568(7753):571-575 (2019)
Verschueren KHG, Blanchet C, Felix J, Dansercoer A, De Vos D, Bloch Y, Van Beeumen J, Svergun D, Gutsche I, Savvides SN, Verstraete K
RgGuinier 6.1 nm
Dmax 19.0 nm
VolumePorod 765 nm3

SASDFB3 – Human ATP-citrate synthers (ACLY) full length in HBS + Citrate

UniProt ID: P53396-1 (None-None) ATP-citrate synthase
ATP-citrate synthase experimental SAS data
ATP-citrate synthase Kratky plot
Sample: ATP-citrate synthase tetramer, 458 kDa Homo sapiens protein
Buffer: 20mM HEPES, 150mM NaCl, 50mM Tris, 20mM citrate, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 4
Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle. Nature 568(7753):571-575 (2019)
Verschueren KHG, Blanchet C, Felix J, Dansercoer A, De Vos D, Bloch Y, Van Beeumen J, Svergun D, Gutsche I, Savvides SN, Verstraete K
RgGuinier 6.2 nm
Dmax 19.0 nm
VolumePorod 787 nm3

SASDFC3 – Human ATP-citrate synthase (ACLY) full length in HBS + Citrate + Coenzyme-A

UniProt ID: P53396-1 (None-None) ATP-citrate synthase
ATP-citrate synthase experimental SAS data
MULTIFOXS model
Sample: ATP-citrate synthase tetramer, 458 kDa Homo sapiens protein
Buffer: 20mM HEPES, 150mM NaCl, 50mM Tris, 20mM citrate, 2mM CoA, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 4
Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle. Nature 568(7753):571-575 (2019)
Verschueren KHG, Blanchet C, Felix J, Dansercoer A, De Vos D, Bloch Y, Van Beeumen J, Svergun D, Gutsche I, Savvides SN, Verstraete K
RgGuinier 5.9 nm
Dmax 17.0 nm
VolumePorod 775 nm3

SASDFD3 – Filamin A Ig-like domains 4-6 (FLNa4-6)

UniProt ID: P21333 (574-869) Filamin A Ig-like domains 4-6
Filamin A Ig-like domains 4-6 experimental SAS data
DAMFILT model
Sample: Filamin A Ig-like domains 4-6 monomer, 32 kDa Homo sapiens protein
Buffer: 20 mM Tris, 100 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2017 Feb 10
Critical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia. Biophys J 117(8):1467-1475 (2019)
Haataja TJK, Capoulade R, Lecointe S, Hellman M, Merot J, Permi P, Pentikäinen U
RgGuinier 2.7 nm
Dmax 9.5 nm
VolumePorod 41 nm3