SASBDB entries for UniProt ID:

SASDDR7 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 2 mg/ml of E248A/E251A C1 in the presence of 1 mM p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1 experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1 Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1 dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 50 mM NaCl, 1 mM HPA, and 5% glycerol, pH: 7
Experiment: SAXS data collected at BL1.3W, Synchrotron Light Research Institute (SLRI) on 2018 May 26
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 2.5 nm
Dmax 8.1 nm
VolumePorod 83 nm3

SASDDS7 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 4 mg/ml of E248A/E251A C1 in the presence of 1 mM p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1 experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1 Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1 dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 50 mM NaCl, 1 mM HPA, and 5% glycerol, pH: 7
Experiment: SAXS data collected at BL1.3W, Synchrotron Light Research Institute (SLRI) on 2018 May 26
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 2.6 nm
Dmax 8.5 nm
VolumePorod 83 nm3

SASDDT7 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 mg/ml of E248A/E251A C1 in the presence of 1 mM p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1 experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1 Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1 dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 50 mM NaCl, 1 mM HPA, and 5% glycerol, pH: 7
Experiment: SAXS data collected at BL1.3W, Synchrotron Light Research Institute (SLRI) on 2018 May 26
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 88 nm3

SASDDU7 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 2 mg/ml of E248A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A mutant
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A mutant Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A 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 2.5 nm
Dmax 7.9 nm
VolumePorod 96 nm3

SASDDV7 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 4 mg/ml of E248A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A mutant
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A mutant Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A 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 2.6 nm
Dmax 8.1 nm
VolumePorod 97 nm3

SASDDW7 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 mg/ml of E248A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A mutant
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A mutant Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A 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 2.5 nm
Dmax 7.9 nm
VolumePorod 94 nm3

SASDDX7 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 2 mg/ml of E248A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A mutant
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A mutant Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A 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 2.7 nm
Dmax 9.0 nm
VolumePorod 94 nm3

SASDDY7 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 4 mg/ml of E248A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A mutant
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A mutant Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A 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 9.0 nm
VolumePorod 91 nm3

SASDDZ7 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 mg/ml of E248A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A mutant
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A mutant Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A 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 2.7 nm
Dmax 8.8 nm
VolumePorod 91 nm3

SASDD28 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 2 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 2.6 nm
Dmax 8.4 nm
VolumePorod 89 nm3