Synchrotron SAXS data from solutions of CRISPR associated Lon protease (CalpL) asymmetrically dimerizing in the presence of cyclic oligoadenylate cA4 in 20 mM Tris, 50 mM NaCl, pH 8 were collected on the EMBL P12 beam line at PETRA III (DESY, Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.155 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.00 mg/ml was measured at 20°C. 30 successive 0.100 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.
The data displayed in this entry shows a SAXS profile measured from a 2 mg/mL sample, as part of a concentration series 2-5 mg/mL with increasing dimer fraction. For 2 mg/mL, the protein is fitted as a mixture, with a 28% volume-fraction of the protein in a dimeric state.
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