Breaking new ground into RAD51–BRC repeats interplay in Homologous Recombination

Rinaldi F Franco P, Veronesi M, Romeo E, Bresciani V, Varignani G, Catalano F, Bernetti M, Masetti M, Langer J, Girotto S, Cavalli A, (2025) DOI

SASDXA5 – DNA repair protein RAD51 homolog 1 (RAD51) [F86E, A89E] in complex with Breast cancer type 2 susceptibility protein (BRCA2) truncation containing the second, third and fourth BRC repeats (BRC2-4) at 2 mg/mL

Breast cancer type 2 susceptibility protein (BRC repeats 2-4)
DNA repair protein RAD51 homolog 1 (F86E A89E)
MWexperimental 139 kDa
MWexpected 150 kDa
VPorod 473 nm3
log I(s) 1.32×10-1 1.32×10-2 1.32×10-3 1.32×10-4
Breast cancer type 2 susceptibility protein (BRC repeats 2-4) DNA repair protein RAD51 homolog 1 (F86E A89E) small angle scattering data  s, nm-1
ln I(s)
Breast cancer type 2 susceptibility protein (BRC repeats 2-4) DNA repair protein RAD51 homolog 1 (F86E A89E) Guinier plot ln 1.32×10-1 Rg: 6.5 nm 0 (6.5 nm)-2 s2
(sRg)2I(s)/I(0)
Breast cancer type 2 susceptibility protein (BRC repeats 2-4) DNA repair protein RAD51 homolog 1 (F86E A89E) Kratky plot 1.104 0 3 sRg
p(r)
Breast cancer type 2 susceptibility protein (BRC repeats 2-4) DNA repair protein RAD51 homolog 1 (F86E A89E) pair distance distribution function Rg: 7.0 nm 0 Dmax: 28.5 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of DNA repair protein RAD51 homolog 1 (RAD51) [F86E, A89E] in complex with Breast cancer type 2 susceptibility protein (BRCA2) truncation containing the second, third and fourth BRC repeats (BRC2-4) at 2 mg/mL in 20 mM K₂HPO₄/KH₂PO₄, 100 mM NaCl, 200 mM Li₂SO₄, 5% glycerol, 1 mM DTT, pH 8 were collected on the B21 beam line at the Diamond Light Source storage ring (Didcot, UK) using a Eiger 4M detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.09464 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.00 mg/ml was measured at 15°C. 21 successive 1 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.

Molecular weight has been inferred through Volume of Correlation (Vc). Sample molecular weight and monodispersity has been independently confirmed through static light scattering (SLS).

Breast cancer type 2 susceptibility protein (BRC repeats 2-4) (BRC2-4)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   38.6 kDa
 
UniProt   P51587 (1212-1551)
Sequence   FASTA
 
DNA repair protein RAD51 homolog 1 (F86E A89E) (RAD51 Trimer)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Trimer
Mon. MW   37.1 kDa
 
UniProt   Q06609 (1-339)
Sequence   FASTA