SASBDB entries for UniProt ID:

SASDUW7 – The tandem SH2 domains of Tyrosine-protein kinase SYK with a bound TYROBP diphospho-ITAM peptide

UniProt ID: P43405 (6-269) Tyrosine-protein kinase SYK

UniProt ID: O43914 (88-107) TYRO protein tyrosine kinase-binding protein
Tyrosine-protein kinase SYKTYRO protein tyrosine kinase-binding protein experimental SAS data
Tyrosine-protein kinase SYK TYRO protein tyrosine kinase-binding protein Kratky plot
Sample: Tyrosine-protein kinase SYK monomer, 30 kDa Homo sapiens protein
TYRO protein tyrosine kinase-binding protein monomer, 2 kDa Homo sapiens protein
Buffer: 10 mM HEPES, 150 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Nov 13
The mechanism of allosteric activation of SYK kinase derived from multiple phospho-ITAM-bound structures Structure (2024)
Bradshaw W, Harris G, Gileadi O, Katis V
RgGuinier 2.1 nm
Dmax 7.1 nm
VolumePorod 53 nm3

SASDUX7 – Aspergillus niger beta-glucosidase (bgl1), partially deglycosylated with Endoglycosidase H

UniProt ID: Q9P8F4 (1-860) beta-glucosidase
beta-glucosidase experimental SAS data
GASBOR model
Sample: Beta-glucosidase dimer, 187 kDa Aspergillus niger protein
Buffer: 50 mM sodium acetate, pH: 5
Experiment: SAXS data collected at 16-ID (LiX), National Synchrotron Light Source II (NSLS-II) on 2024 Feb 15
Aspergillus niger beta-glucosidase (bgl1)
Estella Yee
RgGuinier 4.2 nm
Dmax 14.0 nm
VolumePorod 253 nm3

SASDU78 – Trypanosoma brucei ESAG4 membrane-proximal Venus Fly Trap domain 2 (VFT2)

UniProt ID: Q8WPR6 (480-859) adenylate cyclase
adenylate cyclase experimental SAS data
ALPHAFOLD model
Sample: Adenylate cyclase monomer, 43 kDa Trypanosoma brucei protein
Buffer: 50 mM Tris-HCl, 500 mM NaCl, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2023 Sep 23
Biophysical analysis of the membrane-proximal Venus Flytrap domain of ESAG4 receptor-like adenylate cyclase from Trypanosoma brucei. Mol Biochem Parasitol 260:111653 (2024)
Alves DO, Geens R, da Silva Arruda HR, Jennen L, Corthaut S, Wuyts E, de Andrade GC, Prosdocimi F, Cordeiro Y, Pires JR, Vieira LR, de Oliveira GAP, Sterckx YG, Salmon D
RgGuinier 2.3 nm
Dmax 7.6 nm
VolumePorod 76 nm3

SASDU88 – SEC-SAXS of the fusion protein MPB-MabR(Rv2242) - monomeric peak

UniProt ID: P0AEX9 (27-384) Maltose/maltodextrin-binding periplasmic protein (D108A, K109A, E198A, N199A, K265A)

UniProt ID: P9WPH5 (19-409) Uncharacterized protein Rv2242
Maltose/maltodextrin-binding periplasmic protein (D108A, K109A, E198A, N199A, K265A)Uncharacterized protein Rv2242 experimental SAS data
ALPHAFOLD model
Sample: Maltose/maltodextrin-binding periplasmic protein (D108A, K109A, E198A, N199A, K265A) monomer, 40 kDa Escherichia coli (strain … protein
Uncharacterized protein Rv2242 monomer, 43 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 50 mM Tris pH 7.5, 150 mM NaCl, pH:
Experiment: SAXS data collected at SWING, SOLEIL on 2024 Apr 3
Domain architecture of the Mycobacterium tuberculosis MabR (Rv2242), a member of the PucR transcription factor family Heliyon :e40494 (2024)
Megalizzi V, Tanina A, Grosse C, Mirgaux M, Legrand P, Mirandela G, Wohlkönig A, Bifani P, Wintjens R
RgGuinier 2.8 nm
Dmax 8.5 nm
VolumePorod 113 nm3

SASDU98 – SEC-SAXS of the fusion protein MPB-MabR(Rv2242) - dimeric peak

UniProt ID: P0AEX9 (27-384) Maltose/maltodextrin-binding periplasmic protein (D108A, K109A, E198A, N199A, K265A)

UniProt ID: P9WPH5 (19-409) Uncharacterized protein Rv2242
Maltose/maltodextrin-binding periplasmic protein (D108A, K109A, E198A, N199A, K265A)Uncharacterized protein Rv2242 experimental SAS data
ALPHAFOLD model
Sample: Maltose/maltodextrin-binding periplasmic protein (D108A, K109A, E198A, N199A, K265A) dimer, 80 kDa Escherichia coli (strain … protein
Uncharacterized protein Rv2242 dimer, 86 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 50 mM Tris pH 7.5, 150 mM NaCl, pH:
Experiment: SAXS data collected at SWING, SOLEIL on 2024 Apr 3
Domain architecture of the Mycobacterium tuberculosis MabR (Rv2242), a member of the PucR transcription factor family Heliyon :e40494 (2024)
Megalizzi V, Tanina A, Grosse C, Mirgaux M, Legrand P, Mirandela G, Wohlkönig A, Bifani P, Wintjens R
RgGuinier 3.7 nm
Dmax 10.8 nm
VolumePorod 345 nm3

SASDUA8 – SEC-SAXS of the fusion protein MPB-MabR(Rv2242) - tetrameric peak

UniProt ID: P0AEX9 (27-384) Maltose/maltodextrin-binding periplasmic protein (D108A, K109A, E198A, N199A, K265A)

UniProt ID: P9WPH5 (19-409) Uncharacterized protein Rv2242
Maltose/maltodextrin-binding periplasmic protein (D108A, K109A, E198A, N199A, K265A)Uncharacterized protein Rv2242 experimental SAS data
ALPHAFOLD model
Sample: Maltose/maltodextrin-binding periplasmic protein (D108A, K109A, E198A, N199A, K265A) tetramer, 161 kDa Escherichia coli (strain … protein
Uncharacterized protein Rv2242 tetramer, 171 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 50 mM Tris pH 7.5, 150 mM NaCl, pH:
Experiment: SAXS data collected at SWING, SOLEIL on 2024 Apr 3
Domain architecture of the Mycobacterium tuberculosis MabR (Rv2242), a member of the PucR transcription factor family Heliyon :e40494 (2024)
Megalizzi V, Tanina A, Grosse C, Mirgaux M, Legrand P, Mirandela G, Wohlkönig A, Bifani P, Wintjens R
RgGuinier 5.2 nm
Dmax 15.8 nm
VolumePorod 826 nm3

SASDU29 – The homeodomain of Cone-rod homeobox protein (CRX) bound to Ret4 of the rhodopsin promoter

UniProt ID: O43186 (31-107) Cone-rod homeobox protein

UniProt ID: None (None-None) Ret4 sense strand

UniProt ID: None (None-None) Ret4 antisense strand
Cone-rod homeobox proteinRet4 sense strandRet4 antisense strand experimental SAS data
COOT model
Sample: Cone-rod homeobox protein, 20 kDa Homo sapiens protein
Ret4 sense strand, 6 kDa synthetic construct DNA
Ret4 antisense strand, 6 kDa synthetic construct DNA
Buffer: 20 mM Tris, 150 mM KCl, 5 % glycerol, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Mar 25
Molecular basis of CRX/DNA recognition and stoichiometry at the Ret4 response element Structure (2024)
Srivastava D, Gowribidanur-Chinnaswamy P, Gaur P, Spies M, Swaroop A, Artemyev N
RgGuinier 2.2 nm
Dmax 6.8 nm
VolumePorod 37 nm3

SASDU39 – Nearly full-length monomeric Human Ubiquitin carboxyl-terminal hydrolase 8 (USP8) (7-1110)

UniProt ID: P40818 (7-1110) Ubiquitin carboxyl-terminal hydrolase 8
Ubiquitin carboxyl-terminal hydrolase 8 experimental SAS data
DAMMIF model
Sample: Ubiquitin carboxyl-terminal hydrolase 8 monomer, 127 kDa Homo sapiens protein
Buffer: 25 mM Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2022 Jun 18
Autoinhibition of ubiquitin-specific protease 8: insights into domain interactions and mechanisms of regulation Journal of Biological Chemistry :107727 (2024)
Caba C, Black M, Liu Y, DaDalt A, Mallare J, Fan L, Harding R, Wang Y, Vacratsis P, Huang R, Zhuang Z, Tong Y
RgGuinier 8.4 nm
Dmax 31.8 nm
VolumePorod 327 nm3

SASDU79 – BRUTUS-LIKE2 N-Terminal Region (BTSL2-N)

UniProt ID: F4IDY5 (1-831) Zinc finger protein BRUTUS-like At1g18910
Zinc finger protein BRUTUS-like At1g18910 experimental SAS data
ALPHAFOLD model
Sample: Zinc finger protein BRUTUS-like At1g18910 monomer, 98 kDa Arabidopsis thaliana protein
Buffer: 10 mM MES, 15 mM NaCl, pH: 6.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2023 Feb 8
Iron-sensing and redox properties of the hemerythrin-like domains of Arabidopsis BRUTUS and BRUTUS-LIKE2 proteins. Nat Commun 16(1):3865 (2025)
Pullin J, Rodríguez-Celma J, Franceschetti M, Mundy JEA, Svistunenko DA, Bradley JM, Le Brun NE, Balk J
RgGuinier 3.4 nm
Dmax 9.8 nm
VolumePorod 162 nm3

SASDUY9 – BAM2 in 100 mM KCl (0.25 mg/mL)

UniProt ID: O65258 (56-542) Beta-amylase 2, chloroplastic
Beta-amylase 2, chloroplastic experimental SAS data
Beta-amylase 2, chloroplastic Kratky plot
Sample: Beta-amylase 2, chloroplastic tetramer, 229 kDa Arabidopsis thaliana protein
Buffer: 50 mM HEPES, 100 mM KCl, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Sep 17
Potassium cations expand the conformation ensemble of Arabidopsis thaliana β-amylase2 (BAM2). MicroPubl Biol 2024 (2024)
Sholes A, Asongakap R, Jaconski S, Monroe J, Berndsen CE
RgGuinier 4.9 nm
Dmax 16.4 nm
VolumePorod 226 nm3