Browse by MACROMOLECULE type: protein

SASDD95 – Neurexin 1a L5L6

Neurexin 1a L5L6 experimental SAS data
Neurexin 1a L5L6 Rg histogram
Sample: Neurexin 1a L5L6 monomer, 44 kDa protein
Buffer: 20 mM HEPES pH 8, 150 mM NaCl, 0.5mM CaCl2, pH: 8
Experiment: SAXS data collected at Rigaku BioSAXS-1000, Sealy Center For Structural Biology, UTMB-G on 2016 Sep 6
Structural Plasticity of Neurexin 1α: Implications for its Role as Synaptic Organizer. J Mol Biol 430(21):4325-4343 (2018)
Liu J, Misra A, Reddy MVVVS, White MA, Ren G, Rudenko G
RgGuinier 3.0 nm
Dmax 10.0 nm
VolumePorod 69 nm3

SASDDA5 – Neurexin 1a L5L6 with ss6 insert

Neurexin 1a L5L6 with ss6 insert experimental SAS data
Neurexin 1a L5L6 with ss6 insert Rg histogram
Sample: Neurexin 1a L5L6 with ss6 insert monomer, 45 kDa Homo sapiens protein
Buffer: 20 mM HEPES pH 8, 150 mM NaCl, 0.5mM CaCl2, pH: 8
Experiment: SAXS data collected at Rigaku BioSAXS-1000, Sealy Center For Structural Biology, UTMB-G on 2016 Sep 26
Structural Plasticity of Neurexin 1α: Implications for its Role as Synaptic Organizer. J Mol Biol 430(21):4325-4343 (2018)
Liu J, Misra A, Reddy MVVVS, White MA, Ren G, Rudenko G
RgGuinier 3.2 nm
Dmax 12.4 nm
VolumePorod 70 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