| MWI(0) | 12 | kDa |
| MWexpected | 21 | kDa |
| VPorod | 15 | nm3 |
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log I(s)
9.97×10-3
9.97×10-4
9.97×10-5
9.97×10-6
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s, nm-1
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Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis.
Smith RP, Whitten AE, Paxman JJ, Kahler CM, Scanlon MJ, Heras B, Acta Crystallogr F Struct Biol Commun 74(Pt 1):31-38 (2018) Europe PMCSASDCJ7 – C-terminal domain of DsbD from N. meningitidis
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 solutions of the c-terminal domain of DsbD from Neisseria meningitidis in 25 mM HEPES 150mM NaCl pH 6.7 were collected on the SAXS/WAXS beam line of the Australian Synchrotron (Melbourne, Australia) using a 2D Photon counting Pilatus 1M-W pixel detector (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle; λ=0.1127 nm). Thirty successive 2 second frames were collected across solute concentrations of 0.3-4.5 mg/ml. The SAXS data displayed this entry was derived from a 1.12 mg/ml sample. The change in Rg for c-NmDsbD showed no obvious systematic trend in the concentration range measured. 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.
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