Synchrotron SAXS data from solutions of 20 kDa accessory protein (P20) from Bacillus thuringiensis in 10 mM Tris, 100 mM NaCl, pH 8 were collected on the BL-18 beam line at INDUS-2 (Indore, India) using a MAR 345 Image Plate detector at a sample-detector distance of 2.2 m and at a wavelength of λ = 0.10332 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.20 mg/ml was measured at 25°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
The P20 protein was purified by size exclusion chromatography prior to the SAXS measurement. X-ray exposure time = UNKNOWN.
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