The atypical thiol-disulfide exchange protein α-DsbA2 from Wolbachia pipientis is a homotrimeric disulfide isomerase.
Walden PM,
Whitten AE,
Premkumar L,
Halili MA,
Heras B,
King GJ,
Martin JL
Acta Crystallogr D Struct Biol
75(Pt 3):283-295
(2019 Mar 1)
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Sample: |
DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) trimer, 81 kDa Wolbachia endosymbiont of … protein
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Buffer: |
25 mM TRIS, 150 mM NaCl, pH: 7.5 |
Experiment: |
SAXS
data collected at SAXS/WAXS, Australian Synchrotron on 2014 Mar 29
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RgGuinier |
2.8 |
nm |
Dmax |
8.7 |
nm |
VolumePorod |
913 |
nm3 |
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Sample: |
DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein) monomer, 21 kDa Wolbachia endosymbiont of … protein
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Buffer: |
25 mM TRIS, 150 mM NaCl, pH: 7.5 |
Experiment: |
SAXS
data collected at SAXS/WAXS, Australian Synchrotron on 2012 Feb 29
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RgGuinier |
1.9 |
nm |
Dmax |
6.3 |
nm |
VolumePorod |
275 |
nm3 |
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