SASBDB entries for UniProt ID:

SASDEU6 – Polyglutamine-binding protein 1 p.Arg153Serfs*41 (PQBP-1 XLID mutant R153Sfs*41)

UniProt ID: O60828 (1-154) Polyglutamine-binding protein 1 p.Arg153Serfs*41
Polyglutamine-binding protein 1 p.Arg153Serfs*41 experimental SAS data
Polyglutamine-binding protein 1 p.Arg153Serfs*41 (PQBP-1 XLID mutant R153Sfs*41) Rg histogram
Sample: Polyglutamine-binding protein 1 p.Arg153Serfs*41 dimer, 44 kDa Homo sapiens protein
Buffer: Phosphate-buffered saline, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2013 Feb 15
Frameshift PQBP-1 mutants K192Sfs*7 and R153Sfs*41 implicated in X-linked intellectual disability form stable dimers. J Struct Biol (2019)
Rahman SK, Okazawa H, Chen YW
RgGuinier 3.6 nm
Dmax 13.0 nm
VolumePorod 100 nm3

SASDEX6 – Cold-active AMS8 lipase in the presence of calcium (without polyhistidine affinity tag)

UniProt ID: E1B2U7 (1-476) LipAMS8
LipAMS8 experimental SAS data
DAMMIF model
Sample: LipAMS8 monomer, 50 kDa Pseudomonas sp. AMS8 protein
Buffer: 50 mM Tris HCl, 5 mM CaCl2, pH: 8
Experiment: SAXS data collected at BL1.3W, Synchrotron Light Research Institute (SLRI) on 2018 Mar 6
Structural interpretations of a flexible cold-active AMS8 lipase by combining small-angle X-ray scattering and molecular dynamics simulation (SAXS-MD). Int J Biol Macromol (2022)
Yaacob N, Kamonsutthipaijit N, Soontaranon S, Leow TC, Rahman RNZRA, Ali MSM
RgGuinier 2.9 nm
Dmax 9.8 nm
VolumePorod 87 nm3

SASDEY6 – Arabidopsis thaliana anaphase promoting complex/cyclosome subunit 4 (APC4-strep)

UniProt ID: O65418 (1-777) Anaphase Promoting Complex/Cyclosome Subunit 4
Anaphase Promoting Complex/Cyclosome Subunit 4 experimental SAS data
SREFLEX model
Sample: Anaphase Promoting Complex/Cyclosome Subunit 4 dimer, 184 kDa Arabidopsis thaliana protein
Buffer: 10 mM Tris 150 mM NaCl 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2017 Mar 6
Structural Characterisation of the Arabidopsis thaliana APC4
Steven De Gieter
RgGuinier 4.6 nm
Dmax 16.2 nm
VolumePorod 259 nm3

SASDEZ6 – Gamma-crystallin S disulfide-linked dimer

UniProt ID: P22914 (None-None) Gamma-crystallin S
Gamma-crystallin S experimental SAS data
DAMMIN model
Sample: Gamma-crystallin S dimer, 42 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, pH: 7
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2018 Feb 23
The structure and stability of the disulfide-linked γS-crystallin dimer provide insight into oxidation products associated with lens cataract formation. J Mol Biol (2018)
Thorn DC, Grosas AB, Mabbitt PD, Ray NJ, Jackson CJ, Carver JA
RgGuinier 2.4 nm
Dmax 7.5 nm
VolumePorod 45 nm3

SASDE27 – Gamma-crystallin S monomer

UniProt ID: P22914 (None-None) Gamma-crystallin S
Gamma-crystallin S experimental SAS data
CHIMERA model
Sample: Gamma-crystallin S monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, pH: 7
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2018 Feb 23
The structure and stability of the disulfide-linked γS-crystallin dimer provide insight into oxidation products associated with lens cataract formation. J Mol Biol (2018)
Thorn DC, Grosas AB, Mabbitt PD, Ray NJ, Jackson CJ, Carver JA
RgGuinier 1.8 nm
Dmax 5.9 nm
VolumePorod 27 nm3

SASDE37 – Lysine-specific demethylase 5B, KDM5B, in HEPES buffer

UniProt ID: Q9UGL1 (None-None) Lysine-specific demethylase 5B
Lysine-specific demethylase 5B experimental SAS data
DAMFILT model
Sample: Lysine-specific demethylase 5B monomer, 176 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 300 mM NaCl, 5% (v/v) glycerol, 1mM DTT, pH: 7.7
Experiment: SAXS data collected at Xenocs BioXolver L with GeniX3D, University of Copenhagen, Department of Drug Design and Pharmacology on 2018 Oct 24
Molecular architecture of the Jumonji C family histone demethylase KDM5B. Sci Rep 9(1):4019 (2019)
Dorosz J, Kristensen LH, Aduri NG, Mirza O, Lousen R, Bucciarelli S, Mehta V, Sellés-Baiget S, Solbak SMØ, Bach A, Mesa P, Hernandez PA, Montoya G, Nguyen TTTN, Rand KD, Boesen T, Gajhede M
RgGuinier 8.8 nm
Dmax 26.9 nm

SASDE47 – Aldehyde dehydrogenase 16 from Loktanella sp. (LsALDH16): 2 mg/ml

UniProt ID: A0A0Q3EUQ3 (1-766) Aldehyde dehydrogenase 16 from Loktanella sp.
Aldehyde dehydrogenase 16 from Loktanella sp. experimental SAS data
PYMOL model
Sample: Aldehyde dehydrogenase 16 from Loktanella sp. dimer, 161 kDa Loktanella sp. 3ANDIMAR09 protein
Buffer: 20 mM Tris-HCl, 100 mM NaCl, 2.0% glycerol, 0.5 mM Tris(3-hydroxypropyl)phosphine, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2017 Dec 13
Crystal Structure of Aldehyde Dehydrogenase 16 Reveals Trans-Hierarchical Structural Similarity and a New Dimer. J Mol Biol (2018)
Liu LK, Tanner JJ
RgGuinier 3.6 nm
Dmax 10.9 nm
VolumePorod 202 nm3

SASDE57 – Aldehyde dehydrogenase 16 from Loktanella sp. (LsALDH16): 4 mg/ml

UniProt ID: A0A0Q3EUQ3 (1-766) Aldehyde dehydrogenase 16 from Loktanella sp.
Aldehyde dehydrogenase 16 from Loktanella sp. experimental SAS data
PYMOL model
Sample: Aldehyde dehydrogenase 16 from Loktanella sp. dimer, 161 kDa Loktanella sp. 3ANDIMAR09 protein
Buffer: 20 mM Tris-HCl, 100 mM NaCl, 2.0% glycerol, 0.5 mM Tris(3-hydroxypropyl)phosphine, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2017 Dec 13
Crystal Structure of Aldehyde Dehydrogenase 16 Reveals Trans-Hierarchical Structural Similarity and a New Dimer. J Mol Biol (2018)
Liu LK, Tanner JJ
RgGuinier 3.6 nm
Dmax 11.2 nm
VolumePorod 204 nm3

SASDE67 – Aldehyde dehydrogenase 16 from Loktanella sp. (LsALDH16): 6 mg/ml

UniProt ID: A0A0Q3EUQ3 (1-766) Aldehyde dehydrogenase 16 from Loktanella sp.
Aldehyde dehydrogenase 16 from Loktanella sp. experimental SAS data
PYMOL model
Sample: Aldehyde dehydrogenase 16 from Loktanella sp. dimer, 161 kDa Loktanella sp. 3ANDIMAR09 protein
Buffer: 20 mM Tris-HCl, 100 mM NaCl, 2.0% glycerol, 0.5 mM Tris(3-hydroxypropyl)phosphine, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2017 Dec 13
Crystal Structure of Aldehyde Dehydrogenase 16 Reveals Trans-Hierarchical Structural Similarity and a New Dimer. J Mol Biol (2018)
Liu LK, Tanner JJ
RgGuinier 3.5 nm
Dmax 10.6 nm
VolumePorod 207 nm3

SASDE77 – Aldehyde dehydrogenase 16 from Loktanella sp. (LsALDH16): 8 mg/ml

UniProt ID: A0A0Q3EUQ3 (1-766) Aldehyde dehydrogenase 16 from Loktanella sp.
Aldehyde dehydrogenase 16 from Loktanella sp. experimental SAS data
PYMOL model
Sample: Aldehyde dehydrogenase 16 from Loktanella sp. dimer, 161 kDa Loktanella sp. 3ANDIMAR09 protein
Buffer: 20 mM Tris-HCl, 100 mM NaCl, 2.0% glycerol, 0.5 mM Tris(3-hydroxypropyl)phosphine, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2017 Dec 13
Crystal Structure of Aldehyde Dehydrogenase 16 Reveals Trans-Hierarchical Structural Similarity and a New Dimer. J Mol Biol (2018)
Liu LK, Tanner JJ
RgGuinier 3.6 nm
Dmax 10.8 nm
VolumePorod 205 nm3