BRCA2-HSF2BP oligomeric ring disassembly by BRME1 promotes homologous recombination.

Ghouil R, Miron S, Sato K, Ristic D, van Rossum-Fikkert SE, Legrand P, Ouldali M, Winter JM, Ropars V, David G, Arteni AA, Wyman C, Knipscheer P, Kanaar R, Zelensky AN, Zinn-Justin S, Sci Adv 9(43):eadi7352 (2023) Europe PMC

SASDSM7 – Full-length Heat shock factor 2-binding protein (HSF2BP)

Heat shock factor 2-binding protein
MWI(0) 156 kDa
MWexpected 150 kDa
VPorod 364 nm3
log I(s) 1.31×10-1 1.31×10-2 1.31×10-3 1.31×10-4
Heat shock factor 2-binding protein small angle scattering data  s, nm-1
ln I(s)
Heat shock factor 2-binding protein Guinier plot ln 1.31×10-1 Rg: 8.5 nm 0 (8.5 nm)-2 s2
(sRg)2I(s)/I(0)
Heat shock factor 2-binding protein Kratky plot 1.104 0 3 sRg
p(r)
Heat shock factor 2-binding protein pair distance distribution function Rg: 8.2 nm 0 Dmax: 25 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of full-length HSF2BP in 25 mM Tris-HCl pH 7.5, 250 mM NaCl, 5 mM β-mercaptoethanol were collected on the SWING beam line at SOLEIL (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.103 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 50.00 μl sample at 6 mg/ml was injected at a 0.20 ml/min flow rate onto a Agilent Bio SEC-3, 100 Å column at 293.2°C. 36 successive 0.990 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.

Heat shock factor 2-binding protein (HSF2B_HUMAN)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Tetramer
Mon. MW   37.6 kDa
 
UniProt   O75031 (2-334)
Sequence   FASTA