Multivalent interactions of the disordered regions of XLF and XRCC4 foster robust cellular NHEJ and drive the formation of ligation-boosting condensates in vitro.

Vu DD, Bonucci A, Brenière M, Cisneros-Aguirre M, Pelupessy P, Wang Z, Carlier L, Bouvignies G, Cortes P, Aggarwal AK, Blackledge M, Gueroui Z, Belle V, Stark JM, Modesti M, Ferrage F, Nat Struct Mol Biol (2024) Europe PMC

SASDU67 – The C-terminal region of DNA repair protein XRCC4

DNA repair protein XRCC4
MWexperimental 27 kDa
MWexpected 15 kDa
VPorod 41 nm3
log I(s) 7.30×10-2 7.30×10-3 7.30×10-4 7.30×10-5
DNA repair protein XRCC4 small angle scattering data  s, nm-1
ln I(s)
DNA repair protein XRCC4 Guinier plot ln 7.30×10-2 Rg: 3.4 nm 0 (3.4 nm)-2 s2
(sRg)2I(s)/I(0)
DNA repair protein XRCC4 Kratky plot 1.104 0 √3 sRg
p(r)
DNA repair protein XRCC4 pair distance distribution function Rg: 3.5 nm 0 Dmax: 11.1 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of the C-terminal region of DNA repair protein XRCC4 in 20 mM Bis-tris, 150 mM KCl, 1 mM EDTA, 1 mM DTT, pH 6.5 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Eiger 4M detector (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.00 mg/ml was measured at 20°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Wavelength = UNKNOWN. Sample detector distance = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN

Tags: idp
DNA repair protein XRCC4 (XRCC4)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   15.4 kDa
 
UniProt   Q13426 (201-336)
Sequence   FASTA