X-ray synchrotron radiation scattering data from solutions of N terminal affinity tag cleaved (by thrombin) AbfR1 in 20mMHEPES pH7.5, 200mM NaCl were collected on the BM29 beam line on the storage ring ESRF (Grenoble, France) using a 2D Photon counting Pilatus 1M pixel detector (s = 4π sin θ/λ, where 2θ is the scattering angle). Different solute concentrations in the range 2.5-9.00 mg/mL were measured. 10 successive 20 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 and the different curves were scaled for protein concentration. The low angle data collected were merged with the highest concentration high angle data to yield the final composite scattering curve.The analysis was performed using the ATSAS package. The displayed model is an averaged and volume corrected dummy atom representation (DAMFILT) after imposing P2 symmetry.
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