| MWexperimental | 150 | kDa |
| MWexpected | 150 | kDa |
| VPorod | 340 | nm3 |
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log I(s)
1.56×100
1.56×10-1
1.56×10-2
1.56×10-3
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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 PMCSASDBW7 – N-terminal and chromo-ATPase-DBD domains of chromo domain-containing protein 1 (Chd1: 1-1305)
chromodomain helicase DNA binding domain|
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Fits and models
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Synchrotron SAXS data from solutions of the N-terminal and chromo-ATPase-DBD domains of chromo domain-containing protein 1 (Chd1: 1-1305) in 50mM HEPES, 150mM NaCl, pH 7.5 were collected on the X33 beam line at the DORIS 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 0.5 and 4 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.
Saccharomyces cerevisiae Chd1 protein.
Tags:
X33
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