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Overproduction, purification, crystallization and preliminary X‐ray diffraction analysis of Cockayne syndrome protein A in complex with DNA damage‐binding protein 1
Author(s) -
Meulenbroek Elisabeth M.,
Pannu Navraj S.
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111045842
Subject(s) - crystallization , beamline , cockayne syndrome , overproduction , dna , protein crystallization , x ray crystallography , chemistry , crystallography , synchrotron radiation , microbiology and biotechnology , diffraction , biophysics , dna damage , biology , biochemistry , nucleotide excision repair , optics , gene , physics , beam (structure) , organic chemistry
Cockayne syndrome protein A is one of the main components in mammalian transcription coupled repair. Here, the overproduction, purification and crystallization of human Cockayne syndrome protein A in complex with its interacting partner DNA damage binding protein 1 are reported. The complex was coproduced in insect cells, copurified and crystallized using sitting drops with PEG 3350 and sodium citrate as crystallizing agents. The crystals had unit‐cell parameters a = b = 142.03, c = 250.19 Å and diffracted to 2.9 Å resolution on beamline ID14‐1 at the European Synchrotron Radiation Facility.

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