Overproduction, purification, crystallization and preliminary X-ray diffraction analysis of Cockayne syndrome protein A in complex with DNA damage-binding protein 1.
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.
Biophysical Structural Chemistry, Leiden University, Einsteinweg 55, 2333 CC Leiden, The Netherlands.
Elisabeth M
EM
Meulenbroek
Navraj S
NS
Pannu
D003460:Crystallization; D018360:Crystallography, X-Ray; D045643:DNA Repair Enzymes / Q000737:chemistry* / Q000302:isolation & purification; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000302:isolation & purification; D006801:Humans; D011485:Protein Binding; D014157:Transcription Factors / Q000737:chemistry* / Q000302:isolation & purification
C091435:DDB1 protein, human; D004268:DNA-Binding Proteins; C095472:ERCC8 protein, human; D014157:Transcription Factors; D045643:DNA Repair Enzymes