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47 hits found for Yuenyao

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

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)

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)

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

SASDDW3 – p-hydroxyphenylacetate 3-hydroxylase, reductase component: 2 mg/ml of Wild-type C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

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, 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 85 nm3

SASDDX3 – p-hydroxyphenylacetate 3-hydroxylase, reductase component: 4 mg/ml of Wild-type C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

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, 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 2.7 nm
Dmax 8.6 nm
VolumePorod 95 nm3

SASDDY3 – p-hydroxyphenylacetate 3-hydroxylase, reductase component: 8 mg/ml of Wild-type C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

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, 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 2.7 nm
Dmax 8.9 nm
VolumePorod 102 nm3

SASDDZ3 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 2 mg/ml of H170A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component H170A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component H170A mutant Kratky plot
Sample: p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component H170A 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 7.0 nm
VolumePorod 97 nm3

SASDD24 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 4 mg/ml of H170A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component H170A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component H170A mutant Kratky plot
Sample: p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component H170A 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 7.1 nm
VolumePorod 116 nm3

SASDD34 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 mg/ml of H170A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component H170A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component H170A mutant Kratky plot
Sample: p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component H170A 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 7.0 nm
VolumePorod 98 nm3

SASDD44 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 2 mg/ml of H170A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component H170A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component H170A mutant Kratky plot
Sample: p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component H170A 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 2.6 nm
Dmax 8.6 nm
VolumePorod 85 nm3

SASDD54 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 4 mg/ml of H170A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component H170A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component H170A mutant Kratky plot
Sample: p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component H170A 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 9.0 nm
VolumePorod 107 nm3

SASDD64 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 mg/ml of H170A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component H170A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component H170A mutant Kratky plot
Sample: p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component H170A 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 2.7 nm
Dmax 9.0 nm
VolumePorod 106 nm3

SASDD74 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 2 mg/ml of S172A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component S172A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component S172A mutant Kratky plot
Sample: p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component S172A 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 6.7 nm
VolumePorod 98 nm3

SASDD84 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 4 mg/ml of S172A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component S172A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component S172A mutant Kratky plot
Sample: p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component S172A 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 7.1 nm
VolumePorod 111 nm3

SASDD94 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 mg/ml of S172A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component S172A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component S172A mutant Kratky plot
Sample: p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component S172A 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 7.2 nm
VolumePorod 106 nm3

SASDDA4 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 2 mg/ml of S172A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component S172A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component S172A mutant Kratky plot
Sample: p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component S172A 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 2.7 nm
Dmax 8.2 nm
VolumePorod 83 nm3

SASDDB4 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 4 mg/ml of S172A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component S172A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component S172A mutant Kratky plot
Sample: p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component S172A 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 8.6 nm
VolumePorod 98 nm3

SASDDC4 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 mg/ml of S172A C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component S172A mutant experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component S172A mutant Kratky plot
Sample: p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component S172A 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 8.6 nm
VolumePorod 105 nm3

SASDDD4 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 2 mg/ml of N174A C1 in the absence 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, 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 7.0 nm
VolumePorod 93 nm3

SASDDE4 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 4 mg/ml of N174A C1 in the absence 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, 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 2.6 nm
Dmax 7.6 nm
VolumePorod 96 nm3

SASDDF4 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 mg/ml of N174A C1 in the absence 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, 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 102 nm3

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

SASDDQ7 – p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 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 7.1 nm
VolumePorod 95 nm3

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)

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)

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)

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)

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)

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)

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)

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)

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)

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)

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

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

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)

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)

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)

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)

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