SASDD69 – Medium load concentration of alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) with nicotinamide adenine dinucleotide (NAD) collected by SEC-SAXS

Alpha-aminoadipic semialdehyde dehydrogenase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Alpha-aminoadipic semialdehyde dehydrogenase tetramer, 222 kDa Homo sapiens protein
Buffer: 50 mM Tris, 50 mM NaCl, 0.5 mM DTT, 5% (v/v) glycerol, 1 mM NAD, pH: 7.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Feb 22
NAD+ Promotes Assembly of the Active Tetramer of Aldehyde Dehydrogenase 7A1. FEBS Lett (2018)
Korasick DA, White TA, Chakravarthy S, Tanner JJ
RgGuinier 3.8 nm
VolumePorod 275 nm3

SASDD79 – High load concentration of alpha-aminoadipic semialdehyde dehydrogenase ALDH7A1 with nicotinamide adenine dinucleotide (NAD) collected by SEC-SAXS

Alpha-aminoadipic semialdehyde dehydrogenase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Alpha-aminoadipic semialdehyde dehydrogenase tetramer, 222 kDa Homo sapiens protein
Buffer: 50 mM Tris, 50 mM NaCl, 0.5 mM DTT, 5% (v/v) glycerol, 1 mM NAD, pH: 7.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Feb 22
NAD+ Promotes Assembly of the Active Tetramer of Aldehyde Dehydrogenase 7A1. FEBS Lett (2018)
Korasick DA, White TA, Chakravarthy S, Tanner JJ
RgGuinier 3.8 nm
VolumePorod 277 nm3

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

4101 hits found.