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Synchrotron SAXS data from solutions of Nipah henipavirus W protein in 20 mM HEPES, 150 mM NaCl, 1 M urea, 5 mM DTT, pH 7 were collected on the SWING beam line at SOLEIL (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.1033 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 70.00 μl sample at 2.5 mg/ml was injected at a 0.20 ml/min flow rate onto a Agilent Bio SEC-3, 300 Å column at 20°C. 600 successive 0.990 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
Molecular weight of the Nipah W protein has been determined by MALDI-TOF to 52.657 kDa. Nipah W expressed as a recombinant protein possessing a N-terminal 6xHis tag.
PED: https://proteinensemble.org/PED00205
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s, nm-1
Rg, nm
