Browse by MODEL: No model

SASDDG4 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 4 mg/ml of N174A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component N174A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component N174A mutant Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component N174A mutant dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 5% glycerol, 1 mM HPA, 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 2.8 nm
Dmax 8.7 nm
VolumePorod 94 nm3

SASDDH4 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 mg/ml of N174A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component N174A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component N174A mutant Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component N174A mutant dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 5% glycerol, 1 mM HPA, 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 2.8 nm
Dmax 8.8 nm
VolumePorod 111 nm3

SASDDJ4 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 2 mg/ml of Y207A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component Y207A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component Y207A mutant Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component Y207A mutant 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 104 nm3

SASDDK4 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 4 mg/ml of Y207A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component Y207A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component Y207A mutant Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component Y207A mutant 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 2.5 nm
Dmax 7.1 nm
VolumePorod 111 nm3

SASDDL4 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 mg/ml of Y207A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component Y207A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component Y207A mutant Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component Y207A mutant 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 2.5 nm
Dmax 7.3 nm
VolumePorod 109 nm3

SASDDM4 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 2 mg/ml of Y207A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component Y207A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component Y207A mutant Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component Y207A mutant dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 5% glycerol, 1 mM HPA, 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 7.3 nm
VolumePorod 104 nm3

SASDDN4 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 4 mg/ml of Y207A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component Y207A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component Y207A mutant Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component Y207A mutant dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 5% glycerol, 1 mM HPA, 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 2.5 nm
Dmax 7.2 nm
VolumePorod 122 nm3

SASDDP4 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 mg/ml of Y207A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component Y207A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component Y207A mutant Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component Y207A mutant dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 5% glycerol, 1 mM HPA, 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 106 nm3

SASDDN7 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 2 mg/ml of E248A/E251A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

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, 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 2.3 nm
Dmax 6.7 nm
VolumePorod 88 nm3

SASDDP7 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 4 mg/ml of E248A/E251A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

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, 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 2.4 nm
Dmax 6.8 nm
VolumePorod 90 nm3