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Synchrotron SAXS data from solutions of DNA repair protein RAD51 homolog 3 (Isoform 1) bound to the DNA repair protein XRCC3 in 10 mM HEPES pH 8, 100 mM NaCl, 2.5 mM ATP, 2.5 mM MgCl2, and 0.1 mM Na3VO4, pH 8 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 4 mg/ml were measured at 20°C. Two successive 1 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 low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.
Human RAD51C-XRCC3 complex solution structure in ATP-stabilized state (the buffer includes ATP, the phosphate mimic vanadate, and MgCl2).
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s, nm-1
