SASBDB entries for UniProt ID:

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

SASDU89 – Apolipoprotein A-I monomer, C-terminally truncated

UniProt ID: P02647 (25-208) Apolipoprotein A-I
Apolipoprotein A-I experimental SAS data
COOT model
Sample: Apolipoprotein A-I monomer, 22 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.1% sodium azide, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2021 Mar 20
The structure of the apolipoprotein A-I monomer provides insights into its oligomerisation and lipid-binding mechanisms Journal of Molecular Biology :169394 (2025)
Tou H, Rosenes Z, Khandokar Y, Zlatic C, Metcalfe R, Mok Y, Morton C, Gooley P, Griffin M
RgGuinier 2.3 nm
Dmax 7.9 nm
VolumePorod 27 nm3

SASDU99 – Apolipoprotein A-I dimer, C-terminally truncated

UniProt ID: P02647 (25-208) Apolipoprotein A-I
Apolipoprotein A-I experimental SAS data
DAMMIF model
Sample: Apolipoprotein A-I dimer, 43 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.1% sodium azide, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2021 Mar 20
The structure of the apolipoprotein A-I monomer provides insights into its oligomerisation and lipid-binding mechanisms Journal of Molecular Biology :169394 (2025)
Tou H, Rosenes Z, Khandokar Y, Zlatic C, Metcalfe R, Mok Y, Morton C, Gooley P, Griffin M
RgGuinier 4.2 nm
Dmax 14.0 nm
VolumePorod 58 nm3

SASDUA9 – Apolipoprotein A-I monomer, C-terminally truncated, triply methionine-oxidised

UniProt ID: P02647 (25-208) Apolipoprotein A-I
Apolipoprotein A-I experimental SAS data
Apolipoprotein A-I Kratky plot
Sample: Apolipoprotein A-I monomer, 22 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.1% sodium azide, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2023 Mar 1
The structure of the apolipoprotein A-I monomer provides insights into its oligomerisation and lipid-binding mechanisms Journal of Molecular Biology :169394 (2025)
Tou H, Rosenes Z, Khandokar Y, Zlatic C, Metcalfe R, Mok Y, Morton C, Gooley P, Griffin M
RgGuinier 2.5 nm
Dmax 8.0 nm
VolumePorod 32 nm3

SASDUB9 – Apolipoprotein A-I monomer, C-terminally truncated, SAXS construct G26R mutant

UniProt ID: P02647 (25-208) Apolipoprotein A-I (G50R)
Apolipoprotein A-I (G50R) experimental SAS data
Apolipoprotein A-I (G50R) Kratky plot
Sample: Apolipoprotein A-I (G50R) monomer, 22 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.1% sodium azide, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2023 Jun 27
The structure of the apolipoprotein A-I monomer provides insights into its oligomerisation and lipid-binding mechanisms Journal of Molecular Biology :169394 (2025)
Tou H, Rosenes Z, Khandokar Y, Zlatic C, Metcalfe R, Mok Y, Morton C, Gooley P, Griffin M
RgGuinier 2.3 nm
Dmax 7.9 nm
VolumePorod 28 nm3

SASDUC9 – Full-length apolipoprotein A-I in complex with antigen-binding fragment 55201

UniProt ID: P02647 (25-267) Apolipoprotein A-I

UniProt ID: None (None-None) Antigen-binding fragment 55201
Apolipoprotein A-IAntigen-binding fragment 55201 experimental SAS data
COOT model
Sample: Apolipoprotein A-I monomer, 28 kDa Homo sapiens protein
Antigen-binding fragment 55201 monomer, 45 kDa Mus musculus protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.1% sodium azide, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2021 Jun 19
The structure of the apolipoprotein A-I monomer provides insights into its oligomerisation and lipid-binding mechanisms Journal of Molecular Biology :169394 (2025)
Tou H, Rosenes Z, Khandokar Y, Zlatic C, Metcalfe R, Mok Y, Morton C, Gooley P, Griffin M
RgGuinier 4.6 nm
Dmax 17.5 nm
VolumePorod 99 nm3