RAD51C-XRCC3 structure and cancer patient mutations define DNA replication roles

Longo M, Roy S, Chen Y, Tomaszowski K, Arvai A, Pepper J, Boisvert R, Kunnimalaiyaan S, Keshvani C, Schild D, Bacolla A, Williams G, Tainer J, Schlacher K
Nature Communications 14(1) (2023 Jul 24)

doi: 10.1038/s41467-023-40096-1
Submitted to SASBDB: 2023 Jun 17
Published in SASBDB:

SASDS36 – Human RAD51C-XRCC3 at pH 8 in the presence of ATP and vanadate, a phosphate mimic

Isoform 1 of DNA repair protein RAD51 homolog 3DNA repair protein XRCC3 experimental SAS data
ITASSER model
Sample: Isoform 1 of DNA repair protein RAD51 homolog 3 monomer, 40 kDa Homo sapiens protein
DNA repair protein XRCC3 monomer, 38 kDa Homo sapiens protein
Buffer: 10 mM HEPES pH 8, 100 mM NaCl, 2.5 mM ATP, 2.5 mM MgCl2, and 0.1 mM Na3VO4, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2017 May 5
RgGuinier 3.6 nm
Dmax 14.0 nm
VolumePorod 132 nm3