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

SASDBX7 – Chromo-ATPase domains of chromo domain-containing protein 1 (Chd1: 133-1010)

chromodomain helicase DNA binding domain
MWexperimental 104 kDa
MWexpected 102 kDa
VPorod 190 nm3
log I(s) 1.44×100 1.44×10-1 1.44×10-2 1.44×10-3
chromodomain helicase DNA binding domain small angle scattering data  s, nm-1
ln I(s)
chromodomain helicase DNA binding domain Guinier plot ln 1.44×100 Rg: 4.1 nm 0 (4.1 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: 4.2 nm 0 Dmax: 16.1 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 chromo-ATPase domains of chromo domain-containing protein 1 (Chd1: 133-1010) in 50mM HEPES, 150mM NaCl, pH 7.5 were collected at 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 0.8 and 13.6 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 domain

The chromo-ATPase domains of Saccharomyces cerevisiae Chd1 protein.

Tags: X33
chromodomain helicase DNA binding domain (Chd1)
Mol. type   Protein
Organism   Saccharomyces cerevisiae
Olig. state   Monomer
Mon. MW   101.7 kDa
 
UniProt   P32657 (133-1010)
Sequence   FASTA