SASBDB entries for UniProt ID:

SASDDK3 – Candida antarctica lipase B - with guanidine-HCl unfolding series, in the presence of dithiothreitol

UniProt ID: P41365 (26-342) Lipase B from Pseudozyma antarctica
Lipase B from Pseudozyma antarctica experimental SAS data
Lipase B from Pseudozyma antarctica Kratky plot
Sample: Lipase B from Pseudozyma antarctica, 33 kDa Moesziomyces antarcticus protein
Buffer: 100 mM NaCl, 20 mM Na2HPO4, 10 mM DTT, pH: 6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jul 29
Machine Learning Methods for X-Ray Scattering Data Analysis from Biomacromolecular Solutions. Biophys J 114(11):2485-2492 (2018)
Franke D, Jeffries CM, Svergun DI
RgGuinier 2.4 nm

SASDDL3 – Folded ribonuclease A (RNAse)

UniProt ID: P61823 (None-None) Ribonuclease pancreatic
Ribonuclease pancreatic experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Ribonuclease pancreatic monomer, 16 kDa Bos taurus protein
Buffer: phosphate buffered saline (PBS), pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jul 29
Machine Learning Methods for X-Ray Scattering Data Analysis from Biomacromolecular Solutions. Biophys J 114(11):2485-2492 (2018)
Franke D, Jeffries CM, Svergun DI
RgGuinier 1.6 nm
Dmax 5.6 nm
VolumePorod 16 nm3

SASDDM3 – Carboyxamidomethylated ribonuclease A (unfolded RNAse) - with and without urea

UniProt ID: P61823 (None-None) Ribonuclease pancreatic
Ribonuclease pancreatic experimental SAS data
Ribonuclease pancreatic Kratky plot
Sample: Ribonuclease pancreatic monomer, 16 kDa Bos taurus protein
Buffer: 10 mM HCl, pH: 1
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jul 29
Machine Learning Methods for X-Ray Scattering Data Analysis from Biomacromolecular Solutions. Biophys J 114(11):2485-2492 (2018)
Franke D, Jeffries CM, Svergun DI
RgGuinier 2.3 nm
Dmax 9.0 nm

SASDDN3 – Bovine serum albumin mixture: averaged and individual data frames (subtracted and unsubtracted test sets)

UniProt ID: P02769 (25-607) Bovine serum albumin
Bovine serum albumin experimental SAS data
Bovine serum albumin Kratky plot
Sample: Bovine serum albumin, 66 kDa Bos taurus protein
Buffer: 50 mM HEPES, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Sep 25
Machine Learning Methods for X-Ray Scattering Data Analysis from Biomacromolecular Solutions. Biophys J 114(11):2485-2492 (2018)
Franke D, Jeffries CM, Svergun DI
RgGuinier 3.0 nm
Dmax 11.0 nm
VolumePorod 117 nm3

SASDDP3 – N-propargyl glycine-Inactivated Proline utilization A from Bradyrhizobium diazoefficiens (formerly Bradyrhizobium japonicum) collected by SEC-SAXS

UniProt ID: Q89E26 (None-None) Bifunctional protein PutA
Bifunctional protein PutA experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Bifunctional protein PutA dimer, 215 kDa Bradyrhizobium diazoefficiens protein
Buffer: 50 mM Tris, 50 mM NaCl, 0.5 mM TCEP, 5% (v/v) glycerol, pH: 7.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2017 Jul 16
Redox Modulation of Oligomeric State in Proline Utilization A. Biophys J 114(12):2833-2843 (2018)
Korasick DA, Campbell AC, Christgen SL, Chakravarthy S, White TA, Becker DF, Tanner JJ
RgGuinier 4.6 nm
Dmax 14.4 nm
VolumePorod 324 nm3

SASDDQ3 – Proline utilization A from Bradyrhizobium diazoefficiens (formerly Bradyrhizobium japonicum) collected by SEC-SAXS

UniProt ID: Q89E26 (None-None) Bifunctional protein PutA
Bifunctional protein PutA experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Bifunctional protein PutA tetramer, 430 kDa Bradyrhizobium diazoefficiens protein
Buffer: 50 mM Tris, 50 mM NaCl, 0.5 mM TCEP, 5% (v/v) glycerol, pH: 7.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2017 Jul 16
Redox Modulation of Oligomeric State in Proline Utilization A. Biophys J 114(12):2833-2843 (2018)
Korasick DA, Campbell AC, Christgen SL, Chakravarthy S, White TA, Becker DF, Tanner JJ
RgGuinier 5.2 nm
Dmax 14.2 nm
VolumePorod 582 nm3

SASDDR3 – Yeast tRNA Nm34 methyltransferase Trm7-Trm734 complex from Sacharomyces cerevisiae

UniProt ID: P38238 (1-310) Trm7: tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase

UniProt ID: Q08924 (1-1013) Trm734: Regulator of Ty1 transposition protein 10
Trm7: tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferaseTrm734: Regulator of Ty1 transposition protein 10 experimental SAS data
CORAL model
Sample: Trm7: tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase monomer, 36 kDa Saccharomyces cerevisiae protein
Trm734: Regulator of Ty1 transposition protein 10 monomer, 116 kDa Saccharomyces cerevisiae protein
Buffer: 50 mM HEPES, 200 mM KCl, 5% v/v Glycerol, 10mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2015 Dec 16
Structure of tRNA methyltransferase complex of Trm7 and Trm734 reveals a novel binding interface for tRNA recognition. Nucleic Acids Res (2019)
Hirata A, Okada K, Yoshii K, Shiraishi H, Saijo S, Yonezawa K, Shimizu N, Hori H
RgGuinier 3.8 nm
Dmax 13.0 nm
VolumePorod 218 nm3

SASDDT3 – p-hydroxyphenylacetate 3-hydroxylase, reductase component: 2 mg/ml of wild-type C1 in the absence of p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase, reductase component
p-hydroxyphenylacetate 3-hydroxylase, reductase component experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase, reductase component Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase, reductase component dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, and 5% glycerol, pH: 7
Experiment: SAXS data collected at BL1.3W, Synchrotron Light Research Institute (SLRI) on 2017 Mar 7
Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands. Arch Biochem Biophys 653:24-38 (2018)
Yuenyao A, Petchyam N, Kamonsutthipaijit N, Chaiyen P, Pakotiprapha D
RgGuinier 2.4 nm
Dmax 6.9 nm
VolumePorod 94 nm3

SASDDU3 – p-hydroxyphenylacetate 3-hydroxylase, reductase component: 4 mg/ml of Wild-type C1 in the absence of p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase, reductase component
p-hydroxyphenylacetate 3-hydroxylase, reductase component experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase, reductase component Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase, reductase component dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, and 5% glycerol, pH: 7
Experiment: SAXS data collected at BL1.3W, Synchrotron Light Research Institute (SLRI) on 2017 Mar 7
Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands. Arch Biochem Biophys 653:24-38 (2018)
Yuenyao A, Petchyam N, Kamonsutthipaijit N, Chaiyen P, Pakotiprapha D
RgGuinier 2.4 nm
Dmax 7.1 nm
VolumePorod 95 nm3

SASDDV3 – p-hydroxyphenylacetate 3-hydroxylase, reductase component: 8 mg/ml of Wild-type C1 in the absence of p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase, reductase component
p-hydroxyphenylacetate 3-hydroxylase, reductase component experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase, reductase component Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase, reductase component dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, and 5% glycerol, pH: 7
Experiment: SAXS data collected at BL1.3W, Synchrotron Light Research Institute (SLRI) on 2017 Mar 7
Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands. Arch Biochem Biophys 653:24-38 (2018)
Yuenyao A, Petchyam N, Kamonsutthipaijit N, Chaiyen P, Pakotiprapha D
RgGuinier 2.4 nm
Dmax 7.2 nm
VolumePorod 95 nm3