SASBDB entries for UniProt ID:

SASDD38 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 4 mg/ml of E251A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 50 mM NaCl, 10 % glycerol, pH: 7
Experiment: SAXS data collected at BL1.3W, Synchrotron Light Research Institute (SLRI) on 2018 Apr 25
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 2.7 nm
Dmax 8.9 nm
VolumePorod 93 nm3

SASDD48 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 mg/ml of E251A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 50 mM NaCl, 10 % glycerol, pH: 7
Experiment: SAXS data collected at BL1.3W, Synchrotron Light Research Institute (SLRI) on 2018 Apr 25
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 2.7 nm
Dmax 8.8 nm
VolumePorod 92 nm3

SASDD58 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 2 mg/ml of E251A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 50 mM NaCl, 1 mM HPA, 10 % glycerol, pH: 7
Experiment: SAXS data collected at BL1.3W, Synchrotron Light Research Institute (SLRI) on 2018 Apr 25
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 2.8 nm
Dmax 8.9 nm
VolumePorod 86 nm3

SASDD68 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 4 mg/ml of E251A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 50 mM NaCl, 1 mM HPA, 10 % glycerol, pH: 7
Experiment: SAXS data collected at BL1.3W, Synchrotron Light Research Institute (SLRI) on 2018 Apr 25
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 2.9 nm
Dmax 9.5 nm
VolumePorod 82 nm3

SASDD78 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 mg/ml of E251A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E251A mutant dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 50 mM NaCl, 1 mM HPA, 10 % glycerol, pH: 7
Experiment: SAXS data collected at BL1.3W, Synchrotron Light Research Institute (SLRI) on 2018 Apr 25
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 2.9 nm
Dmax 9.3 nm
VolumePorod 89 nm3

SASDD98 – Apolipoprotein E3

UniProt ID: P02649 (19-317) Apolipoprotein E3
Apolipoprotein E3 experimental SAS data
Apolipoprotein E3 Kratky plot
Sample: Apolipoprotein E3 tetramer, 139 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 300 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Nov 29
The molecular basis for Apolipoprotein E4 as the major risk factor for late onset Alzheimer's disease. J Mol Biol (2019)
Raulin AC, Kraft L, Al-Hilaly YK, Xue WF, McGeehan JE, Atack JR, Serpell L
RgGuinier 5.7 nm
Dmax 19.5 nm
VolumePorod 410 nm3

SASDDA8 – Apolipoprotein E4

UniProt ID: P02649 (19-317) Apolipoprotein E4
Apolipoprotein E4 experimental SAS data
Apolipoprotein E4 Kratky plot
Sample: Apolipoprotein E4 tetramer, 139 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 300 mM NaCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Nov 29
The molecular basis for Apolipoprotein E4 as the major risk factor for late onset Alzheimer's disease. J Mol Biol (2019)
Raulin AC, Kraft L, Al-Hilaly YK, Xue WF, McGeehan JE, Atack JR, Serpell L
RgGuinier 5.8 nm
Dmax 19.6 nm
VolumePorod 430 nm3

SASDDB8 – Periplasmic domain of inner membrane protein GspL, dimer

UniProt ID: P25060 (261-382) Type II secretion system protein L, periplasmic domain
Type II secretion system protein L, periplasmic domain experimental SAS data
EOM/RANCH model
Sample: Type II secretion system protein L, periplasmic domain dimer, 28 kDa Pseudomonas aeruginosa protein
Buffer: 50 mM TRIS, 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2016 Apr 8
Structure and oligomerization of the periplasmic domain of GspL from the type II secretion system of Pseudomonas aeruginosa. Sci Rep 8(1):16760 (2018)
Fulara A, Vandenberghe I, Read RJ, Devreese B, Savvides SN
RgGuinier 2.2 nm
Dmax 7.5 nm

SASDDC8 – Periplasmic domain of inner membrane protein GspL, tetramer

UniProt ID: P25060 (261-382) Type II secretion system protein L, periplasmic domain
Type II secretion system protein L, periplasmic domain experimental SAS data
Type II secretion system protein L, periplasmic domain Kratky plot
Sample: Type II secretion system protein L, periplasmic domain dimer, 28 kDa Pseudomonas aeruginosa protein
Buffer: 50 mM TRIS, 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2016 Apr 8
Structure and oligomerization of the periplasmic domain of GspL from the type II secretion system of Pseudomonas aeruginosa. Sci Rep 8(1):16760 (2018)
Fulara A, Vandenberghe I, Read RJ, Devreese B, Savvides SN
RgGuinier 3.2 nm
Dmax 10.5 nm

SASDDE8 – Integrin beta4, fragment of the cytoplasmic region that includes the final part of the connecting segment and the third and fourth FnIII domains (FnIII-3,4)

UniProt ID: P16144-2 (1436-1666) Integrin beta-4 fragment with final part of the connecting segment and the third and fourth FnIII domains
Integrin beta-4 fragment with final part of the connecting segment and the third and fourth FnIII domains experimental SAS data
Integrin beta4, fragment of the cytoplasmic region that includes the final part of the connecting segment and the third and fourth FnIII domains (FnIII-3,4) Rg histogram
Sample: Integrin beta-4 fragment with final part of the connecting segment and the third and fourth FnIII domains monomer, 26 kDa Homo sapiens protein
Buffer: 20 mM Sodium Phosphate 150 mM NaCl 5% glycerol 3 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 26
Integrin α6β4 Recognition of a Linear Motif of Bullous Pemphigoid Antigen BP230 Controls Its Recruitment to Hemidesmosomes. Structure 27(6):952-964.e6 (2019)
Manso JA, Gómez-Hernández M, Carabias A, Alonso-García N, García-Rubio I, Kreft M, Sonnenberg A, de Pereda JM
RgGuinier 2.4 nm
Dmax 9.5 nm
VolumePorod 37 nm3