Browse by MODEL: No model

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

SASDCZ8 – Human Rev7 dimer in complex with Rev3 peptide @ 12.2 mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.8 nm

SASDC49 – Human Rev7 dimer in complex with Rev3 peptide @ 6.1mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 3.1 nm
Dmax 11.6 nm
VolumePorod 105 nm3

SASDC59 – Human Rev7 dimer in complex with Rev3 peptide @ 7.6mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.9 nm
Dmax 11.1 nm
VolumePorod 106 nm3

SASDC69 – Human Rev7 dimer in complex with Rev3 peptide @ 4.6mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.9 nm