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Synchrotron SAXS data from solutions of Plasmodium falciparum Hsp70/Hsp90 organizing protein, Hop in 25 mM Tris-HCl, 100 mM NaCl, 1 mM EDTA, 1 mM β-mercaptoethanol, pH 8 were collected on the SAXS1 beam line at the Brazilian Synchrotron Light Laboratory (Campinas, Brazil) using a Pilatus 300K detector at a sample-detector distance of 0.9 m and at a wavelength of λ = 0.1488 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 2.8 mg/ml were measured . The X-ray exposure times were 6 x 10 sec and 1 x 100 sec for all samples. 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 concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.
Top: The model represents the averaged spatial disposition (volume and bead-occupancy corrected; damfilt model) obtained from several spatially aligned individual dummy atom model (DAM) reconstructions calculated using DAMMIF. Bottom: A single DAMMIF representative model with the lowest NSD from the aligned DAM cohort. The corresponding fit to the SAXS data is displayed.
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s, nm-1
