Molecular basis of histone tail recognition by human TIP5 PHD finger and bromodomain of the chromatin remodeling complex NoRC.

Tallant C, Valentini E, Fedorov O, Overvoorde L, Ferguson FM, Filippakopoulos P, Svergun DI, Knapp S, Ciulli A, Structure 23(1):80-92 (2015) Europe PMC

SASDA66 – BAZ2B-18mer complex in Tris

Bromodomain adjacent to zinc finger domain protein 2B, C-terminal
H3Kac9Kac14
MWI(0) 45 kDa
MWexpected 32 kDa
VPorod 52 nm3
log I(s) 3.75×101 3.75×100 3.75×10-1 3.75×10-2
Bromodomain adjacent to zinc finger domain protein 2B, C-terminal H3Kac9Kac14 small angle scattering data  s, nm-1
ln I(s)
Bromodomain adjacent to zinc finger domain protein 2B, C-terminal H3Kac9Kac14 Guinier plot ln 3.75×101 Rg: 4.2 nm 0 (4.2 nm)-2 s2
(sRg)2I(s)/I(0)
Bromodomain adjacent to zinc finger domain protein 2B, C-terminal H3Kac9Kac14 Kratky plot 1.104 0 3 sRg
p(r)
Bromodomain adjacent to zinc finger domain protein 2B, C-terminal H3Kac9Kac14 pair distance distribution function Rg: 4.5 nm 0 Dmax: 16 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of BAZ2B-18mer complex in Tris in 20 mM Tris 500 mM NaCl 2 mM DTT 10 microM ZnCl2, pH 8 were collected on the EMBL X33 beam line at the DORIS III, DESY 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). One solute concentration of 2.75 mg/ml was 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.

Tags: X33
Bromodomain adjacent to zinc finger domain protein 2B, C-terminal (BAZ2B)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   27.7 kDa
Sequence   FASTA
 
H3Kac9Kac14 (peptide 18mer)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   4.7 kDa
Sequence   FASTA