Synchrotron SAXS data from solutions of a chimeric EcRHH-RcPutA protein fusion in 50 mM Tris, 200 mM NaCl, 0.5 mM Tris(3-hydroxypropyl)phosphine, pH 7.5 were collected on the 12.3.1 (SIBYLS) camera on the storage ring Advanced Light Source (ALS) (Berkeley, CA, USA) using a MAR 165 CCD detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle). A solute concentrations of 6 mg/ml was measured at 20°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The merged SAXS curve displayed in this entry was obtained by merging the low-s region (points 2-140, s=0.1125 — 0.9517 nm-1) from an image collected with an exposure time of 0.5 s with the higher-s region (points 19-505, s=0.2159 — 3.1710 nm-1) of a profile collected with exposure time of 2.0 s. The errors in PDDF Rg and I0 were estimated by running GNOM via primus/qt (r4556) assuming Dmax in the range of 173-193 and using all points of the scattering curve (1-503).
s, nm-1
