| MWexperimental | 120 | kDa |
| MWexpected | 117 | kDa |
| VPorod | 228 | nm3 |
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log I(s)
1.36×100
1.36×10-1
1.36×10-2
1.36×10-3
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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 PMCSASDBY7 – N-terminal and chromo-ATPase domains of chromo domain-containing protein 1 (Chd1: 1-1010)
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-chromo-ATPase domains of chromo domain-containing protein 1 (Chd1: 1-1010) in 50mM HEPES, 150mM NaCl, pH 7.5 were collected at the X33 beam line on 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 0.6 and 9.8 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.
The protein fragment 1-1010 encompassing the N-terminal and chromo-ATPase domains of Saccharomyces cerevisiae Chd1.
Tags:
X33
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