In vitro characterization of the catalytic domain of HDAC5

Jens Reiners.

SASDXL6 – Histone deacetylase 5 (HDAC5)

Histone deacetylase 5
MWI(0) 50 kDa
MWexpected 51 kDa
VPorod 82 nm3
log I(s) 3.61×10-2 3.61×10-3 3.61×10-4 3.61×10-5
Histone deacetylase 5 small angle scattering data  s, nm-1
ln I(s)
Histone deacetylase 5 Guinier plot ln 3.62×10-2 Rg: 2.8 nm 0 (2.8 nm)-2 s2
(sRg)2I(s)/I(0)
Histone deacetylase 5 Kratky plot 1.104 0 3 sRg
p(r)
Histone deacetylase 5 pair distance distribution function Rg: 2.9 nm 0 Dmax: 10.1 nm

Data validation


There are no models related to this curve.

SAXS data from solutions of Histone deacetylase 5 (HDAC5) in 25 mM HEPES, 150 mM KCl, 1 mM DTT,, pH 7.5 were collected on the Xenocs Xeuss 2.0 Q-Xoom instrument (Center for Structural Studies, Heinrich-Heine-University, Düsseldorf, Germany) using a Pilatus3 R 300K detector at a sample-detector distance of 0.6 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.15 mg/ml was measured at 15°C. 24 successive 600 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.

Histone deacetylase 5 (HDAC5)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   51.1 kDa
 
UniProt   Q9UQL6 (655-1122)
Sequence   FASTA