An integrative structural study of the human full-length RAD52 at 2.2 Å resolution

Balboni B, Marotta R, Rinaldi F, Milordini G, Varignani G, Girotto S, Cavalli A, Communications Biology 7(1) (2024) DOI

SASDQ49 – His-Tagged full length DNA repair protein RAD52 homolog

DNA repair protein RAD52 homolog
MWexperimental 585 kDa
MWexpected 528 kDa
VPorod 1218 nm3
log I(s) 8.76×101 8.76×100 8.76×10-1 8.76×10-2
DNA repair protein RAD52 homolog small angle scattering data  s, nm-1
ln I(s)
DNA repair protein RAD52 homolog Guinier plot ln 8.77×101 Rg: 8.0 nm 0 (8.0 nm)-2 s2
(sRg)2I(s)/I(0)
DNA repair protein RAD52 homolog Kratky plot 1.104 0 √3 sRg
p(r)
DNA repair protein RAD52 homolog pair distance distribution function Rg: 8.8 nm 0 Dmax: 40.2 nm

Data validation

Fits and models

log I(s)
 s, nm-1
His-Tagged full length DNA repair protein RAD52 homolog Rg histogram Rg, nm
DNA repair protein RAD52 homolog EOM/RANCH model
DNA repair protein RAD52 homolog EOM/RANCH model
DNA repair protein RAD52 homolog EOM/RANCH model
DNA repair protein RAD52 homolog EOM/RANCH model
Synchrotron SAXS data from solutions of His-Tagged full length DNA repair protein RAD52 in 20 mM Tris pH 7.5, 250 mM NaCl, 1% glycerol, were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus3 2M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.099 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 1.3 mg/ml was injected at a 0.07 ml/min flow rate onto a GE Superose 6 Increase 3.2/300 column at 20°C. 600 successive 2 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 RAD52 homolog (RAD52)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Undecamer
Mon. MW   48.0 kDa
 
UniProt   P43351 (1-418)
Sequence   FASTA