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