The PHD and chromo domains regulate the ATPase activity of the human chromatin remodeler CHD4.

Watson AA, Mahajan P, Mertens HD, Deery MJ, Zhang W, Pham P, Du X, Bartke T, Zhang W, Edlich C, Berridge G, Chen Y, Burgess-Brown NA, Kouzarides T, Wiechens N, Owen-Hughes T, Svergun DI, Gileadi O, Laue ED, J Mol Biol 422(1):3-17 (2012) Europe PMC


Human Chromatin Remodeler CHD4 (363-682)
MWI(0) 39 kDa
MWexpected 38 kDa
log I(s) 3.81×101 3.81×100 3.81×10-1 3.81×10-2
Human Chromatin Remodeler CHD4 (363-682) small angle scattering data  s, nm-1
ln I(s)
Human Chromatin Remodeler CHD4 (363-682) Guinier plot ln 3.81×101 Rg: 3 nm 0 (3 nm)-2 s2
Human Chromatin Remodeler CHD4 (363-682) Kratky plot 1.104 0 3 sRg
Human Chromatin Remodeler CHD4 (363-682) pair distance distribution function Rg: 3.1 nm 0 Dmax: 10.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Human Chromatin Remodeler CHD4 (363-682) DAMMIF model

Synchrotron SAXS data from solutions of CHD4 (PP-CC) in 50 mM HEPES 50 mM KCl, pH 7.5 were collected on the EMBL X33 beam line at the DORIS III storage ring (Hamburg, Germany) using a Pilatus 1M-W detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.1 and 8.2 mg/ml were measured at 10°C. Eight successive 15 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. 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.

Tags: X33
Human Chromatin Remodeler CHD4 (363-682) (CHD4 (PP-CC))
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   37.8 kDa
Sequence   FASTA