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Synchrotron SAXS data from solutions of Chd1-12N12, chromatin remodeler--nucleosome complex suspended in 60% sucrose without any nucleotides added (Apo), 10 mM Tris, 100 mM NaCl, 2 mM MgCl2, 0.1 mM EDTA, 1 mM DTT, 60% (w/v) sucrose, pH 7.8, were collected on the G1 beam line at the Cornell High Energy Synchrotron Source (Ithaca, NY, USA) using a Pilatus Pilatus 200K detector at a sample-detector distance of 2.1 m and at a wavelength of λ = 0.1109 nm (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle). One solute concentration of 1.88 mg/ml was measured at 25°C. 40 successive 10 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 to produce the scattering profile displayed in this entry.
12N12 nucleosomes in the presence of the chromatin remodeler Chd1 in 60% sucrose and no nucleotides added (apo). The complex formed contains two Chd1 proteins bound to each nucleosome. Due to contrast matching between the solvent and histone proteins, the measured signal is dominated by the DNA component. The models were generated using 3D-DART and custom scripts written in Pymol. The percentage-weighting of each model in the ensemble ('XXXperc') is noted in the following model key/list that sequentially corresponds to models displayed in this entry ordered from top-to-bottom: SASDCU6_fit1_model1 = Chd1_12N12_apo_01_wrapped_27perc;
SASDCU6_fit1_model2 = Chd1_12N12_apo_02_extreme_09perc;
SASDCU6_fit1_model3 = Chd1_12N12_apo_03_wrapped_36perc;
SASDCU6_fit1_model4 = Chd1_12N12_apo_04_inplane_27perc.
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s, nm-1
Rg, nm
