Expression, purification, crystallization and preliminary X‐ray analysis of the RecQ helicase catalytic core from Deinococcus radiodurans

Publisher： John Wiley & Sons Inc

E-ISSN： 1744-3091|68|10|1234-1236

ISSN： 1744-3091

Source： Acta Crystallographica Section F, Vol.68, Iss.10, 2012-10, pp. : 1234-1236

Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.

Previous Menu Next

Abstract

The RecQ proteins are a highly conserved group of DNA helicases which play crucial roles in the maintenance of genome stability. DrRecQ from the radioresistant bacterium Deinococcus radiodurans is a special member of the RecQ family because it contains three Helicase‐and‐RNase‐D‐C‐terminal (HRDC) domains at the C‐terminus. The helicase catalytic core is essential for ATPase and DNA‐unwinding activities. In this work, the helicase catalytic core of DrRecQ was expressed in Escherichia coli, purified and crystallized. Crystals were obtained using the sitting‐drop vapour diffusion method and X‐ray diffraction data were collected to 2.9 Å resolution. The crystals belong to space group P2₁2₁2₁, with unit‐cell parameters a = 84.75, b = 95.61, c = 183.83 Å.