| MWexperimental | 138 | kDa |
| MWexpected | 135 | kDa |
| VPorod | 280 | nm3 |
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log I(s)
9.20×10-1
9.20×10-2
9.20×10-3
9.20×10-4
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s, nm-1
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Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes.
Sundaramoorthy R, Hughes AL, Singh V, Wiechens N, Ryan DP, El-Mkami H, Petoukhov M, Svergun DI, Treutlein B, Quack S, Fischer M, Michaelis J, Böttcher B, Norman DG, Owen-Hughes T, Elife 6 (2017) Europe PMCSASDBV7 – Chromo-ATPase-DBD domains of chromo domain-containing protein 1 (Chd1: 133-1305)
chromodomain helicase DNA binding domain|
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Fits and models
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Synchrotron SAXS data from solutions of the chromo-ATPase-DBD domains from chromo domain-containing protein 1 (Chd1: 133-1305) in 50mM HEPES, 150mM NaCl, pH 7.5 were collected on the P12 beam line at PETRA III storage ring (Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 5 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsin θ/λ and 2θ is the scattering angle). Solute concentrations ranging between 0.2 and 3.5 mg/ml were measured at 10°C. 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 at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.
Chromo-Helicase-DBD of chd1
The chromo-helicase-DNA binding domains of Saccharomyces cerevisiae Chd1. |
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