SASBDB entries for UniProt ID:

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

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

SASDUZ9 – BAM2 in 100 mM KCl (0.5 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 15.0 nm
VolumePorod 234 nm3

SASDV22 – BAM2 in 100 mM KCl (1 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 4.7 nm
Dmax 15.1 nm
VolumePorod 218 nm3