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 PMC

SASDBU7 – DNA binding domain (DBD) of chromo domain-containing protein 1 (Chd1: 1009-1274)

chromodomain helicase DNA binding domain
MWI(0) 32 kDa
MWexpected 31 kDa
log I(s) 3.46×101 3.46×100 3.46×10-1 3.46×10-2
chromodomain helicase DNA binding domain small angle scattering data  s, nm-1
ln I(s)
chromodomain helicase DNA binding domain Guinier plot ln 3.46×101 Rg: 2.6 nm 0 (2.6 nm)-2 s2
(sRg)2I(s)/I(0)
chromodomain helicase DNA binding domain Kratky plot 1.104 0 √3 sRg
p(r)
chromodomain helicase DNA binding domain pair distance distribution function Rg: 2.6 nm 0 Dmax: 8.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
chromodomain helicase DNA binding domain GASBOR model
Synchrotron SAXS data from solutions of the DNA binding domain (DBD) of chromo domain-containing protein 1 (Chd1: 1009-1274) 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 1M-W 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 1.2 and 9.9 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 concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

The DNA binding module of Saccharomyces cerevisiae Chd1 protein.

Tags: X33
chromodomain helicase DNA binding domain (Chd1-DBD)
Mol. type   Protein
Organism   Saccharomyces cerevisiae
Olig. state   Monomer
Mon. MW   31.1 kDa
 
UniProt   P32657 (1009-1274)
Sequence   FASTA