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Preliminary crystallographic studies of BRCA1 BRCT-ABRAXAS complex.

ABSTRACT: 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 P4(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%.

SUBMITTER: Badgujar DC

PROVIDER: S-EPMC3855730 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature

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Preliminary crystallographic studies of BRCA1 BRCT-ABRAXAS complex.

Badgujar Dilip C DC Sawant Ulka U Yadav Lumbini L Hosur M V MV Varma Ashok K AK

Acta crystallographica. Section F, Structural biology and crystallization communications 20131129 Pt 12

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 P4(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 molec ...[more]

PMID: 24316840

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