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

MW^experimental	83	kDa
MW^expected	76	kDa
V^Porod	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

Log plot Log-Log plot

ln I(s)

ln 1.24×10² R_g: 5.4 nm 0 (5.4 nm)^-2 s²

(sR_g)²I(s)/I(0)

1.104 0 √3 sR_g

p(r)	R_g: 5.7 nm 0 D_max: 19.5 nm

Data validation

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

DNA repair protein XRCC1ΔN BILBOMD model

log I(s)	s, nm^-1
+3 Δ/σ -3	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