Synchrotron SAXS data from solutions of the AtFKBP43 (1-136) -H3/H4 histone oligomer complex in 20 mM Tris, 300 mM NaCl, 1 mM β-mercaptoethanol, pH 7.5 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus3 2M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.09794 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 0.50 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 bead models displayed in this entry show an individual DAMMIF model shape reconstruction and associated fit, in addition to the volume/bead occupancy-corrected averaged representation of the protein calculated from the spatial alignment of an individual model cohort consisting of several individual bead models (DAMFILT).
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