Overproduction, purification, crystallization and preliminary X-ray diffraction analysis of Cockayne syndrome protein A in complex with DNA damage-binding protein 1.

Abstract

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.

• Authors: Elisabeth M Meulenbroek, Navraj S Pannu
• Journal: Acta crystallographica. Section F, Structural biology and crystallization communications (Acta Crystallogr Sect F Struct Biol Cryst Commun) Vol. 68 Issue Pt 1 Pg. 45-8 (Jan 01 2012) ISSN: 1744-3091 [Electronic] England
• PMID: 22232169 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: © 2012 International Union of Crystallography. All rights reserved.

Chemical References

• DDB1 protein, human
• DNA-Binding Proteins
• ERCC8 protein, human
• Transcription Factors
• DNA Repair Enzymes

Topics

• Crystallization
• Crystallography, X-Ray
• DNA Repair Enzymes (chemistry, isolation & purification)
• DNA-Binding Proteins (chemistry, isolation & purification)
• Humans
• Protein Binding
• Transcription Factors (chemistry, isolation & purification)