An atypical BRCT-BRCT interaction with the XRCC1 scaffold protein compacts human DNA Ligase IIIα within a flexible DNA repair complex.

Hammel M, Rashid I, Sverzhinsky A, Pourfarjam Y, Tsai MS, Ellenberger T, Pascal JM, Kim IK, Tainer JA, Tomkinson AE, Nucleic Acids Res (2020) Europe PMC

SASDJ52 – DNA repair protein XRCC1ΔN monomer/dimer

DNA repair protein XRCC1ΔN
MWexperimental 83 kDa
MWexpected 76 kDa
VPorod 170 nm3
log I(s) 1.23×102 1.23×101 1.23×100 1.23×10-1
DNA repair protein XRCC1ΔN small angle scattering data  s, nm-1
ln I(s)
DNA repair protein XRCC1ΔN Guinier plot ln 1.24×102 Rg: 5.4 nm 0 (5.4 nm)-2 s2
(sRg)2I(s)/I(0)
DNA repair protein XRCC1ΔN Kratky plot 1.104 0 √3 sRg
p(r)
DNA repair protein XRCC1ΔN pair distance distribution function Rg: 5.7 nm 0 Dmax: 19.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
DNA repair protein XRCC1ΔN BILBOMD model
DNA repair protein XRCC1ΔN BILBOMD model
DNA repair protein XRCC1ΔN BILBOMD model
log I(s)
 s, nm-1
Synchrotron SAXS data from solutions of DNA repair protein XRCC1ΔN in 25 mM Tris-HCl pH 7.5, 150 mM NaCl, 10% glycerol, 2 mM DTT, were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a MAR 165 CCD detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.11 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 5 mg/ml were measured at 20°C. Three successive 0.500 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Storage temperature = UNKNOWN

DNA repair protein XRCC1ΔN (XRCC1ΔN)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   38.0 kDa
 
UniProt   P18887 (294-633)
Sequence   FASTA