| MWI(0) | 23 | kDa |
| MWexpected | 21 | kDa |
| VPorod | 275 | nm3 |
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log I(s)
2.15×10-2
2.15×10-3
2.15×10-4
2.15×10-5
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s, nm-1
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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) Europe PMCSASDC38 – Truncated α-DsbA2 protein
DsbA-like disulfide oxidoreductase (thiol-disulfide exchange protein)|
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Fits and models
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X-ray synchrotron radiation scattering data from the truncated version of α-DsbA2 from Wolbachia pipientis in 25 mM TRIS 150mM NaCl pH 7.5 were collected on the SAXS/WAXS beam line of the Australian Synchrotron (Melbourne, Australia) using a 2D Photon counting Pilatus 1M-W pixel detector (s = 4π sin θ/λ, where 2θ is the scattering angle). Eight successive 2 second frames were collected across solute concentrations of 1.25-5.00 mg/ml. The SAXS data displayed this entry was derived from a 1.25 mg/ml sample. The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering of the solvent-blank was subtracted. The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering of the solvent-blank was subtracted. The models and corresponding fits include those derived from dummy-atom modelling using DAMMIN (top) and rigid-body modelling using CORAL (bottom).
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