Open AccessPreliminary crystallographic studies of BRCA1 BRCT–ABRAXAS complex
Author(s) -
Badgujar Dilip C.,
Sawant Ulka,
Yadav Lumbini,
Hosur M. V.,
Varma Ashok K.
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113030649
Subject(s) - crystallography , crystallization , molecule , materials science , chemistry , stereochemistry , organic chemistry
The BRCA1 holoenzyme complex plays an important role in DNA damage repair. ABRAXAS is a newly discovered component of this complex and its C‐terminal region directly binds to the BRCA1 BRCT domain. Single crystals of the BRCA1 BRCT–ABRAXAS complex grown by co‐crystallization belonged to space group P 4 1 2 1 2, with unit‐cell parameters a = b = 187.18, c = 85.31 Å. Diffraction data were collected on the BM‐14 beamline at the ESRF. Molecular‐replacement calculations using Phaser led to three molecules in the asymmetric unit and a high solvent content of 76%.