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

SASDJ62 – DNA repair protein XRCC1 monomer /dimer

DNA repair protein XRCC1
MWexperimental 110 kDa
MWexpected 69 kDa
VPorod 330 nm3
log I(s) 1.47×102 1.47×101 1.47×100 1.47×10-1
DNA repair protein XRCC1 small angle scattering data  s, nm-1
ln I(s)
DNA repair protein XRCC1 Guinier plot ln 1.47×102 Rg: 6.3 nm 0 (6.3 nm)-2 s2
DNA repair protein XRCC1 Kratky plot 1.104 0 3 sRg
DNA repair protein XRCC1 pair distance distribution function Rg: 7.4 nm 0 Dmax: 26.9 nm

Data validation

Fits and models

log I(s)
 s, nm-1
DNA repair protein XRCC1 BILBOMD model
DNA repair protein XRCC1 BILBOMD model
DNA repair protein XRCC1 BILBOMD model

Synchrotron SAXS data from solutions of DNA repair protein XRCC1 in 200 mM NaCl, 20 mM Tris-HCl, pH 7.5 , 2% glycerol, were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 2.1 m and at a wavelength of λ = 0.1127 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 5.9 mg/ml was injected at a 0.50 ml/min flow rate onto a Shodex KW403 column at 20°C. 600 successive 3 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.

DNA repair protein XRCC1 (XRCC1)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Unknown
Mon. MW   69.5 kDa
UniProt   P18887 (1-633)
Sequence   FASTA