Unknown

Dataset Information

0

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.

SUBMITTER: Meulenbroek EM 

PROVIDER: S-EPMC3253832 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Meulenbroek Elisabeth M EM   Pannu Navraj S NS  

Acta crystallographica. Section F, Structural biology and crystallization communications 20111224 Pt 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  ...[more]

Similar Datasets

| S-EPMC2688435 | biostudies-literature
| S-EPMC2833043 | biostudies-literature
| S-EPMC2998367 | biostudies-literature
| S-EPMC2219979 | biostudies-literature
| S-EPMC2242937 | biostudies-literature
| S-EPMC2344096 | biostudies-literature
| S-EPMC2496858 | biostudies-literature
| S-EPMC2376414 | biostudies-literature
| S-EPMC3151135 | biostudies-literature
| S-EPMC3232156 | biostudies-literature