title: Expression, purification, crystallization and preliminary X-ray analysis of the RecQ helicase catalytic core from Deinococcus radiodurans.
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 P2(1)2(1)2(1), with unit-cell parameters a = 84.75, b = 95.61, c = 183.83 Å.
authors.affiliation: Institute of Biochemistry and Molecular Biology, College of Medicine, National Taiwan University, Taipei City, 100, Taiwan.
authors.forename: Sheng-Chia
authors.initials: SC
authors.lastname: Chen
authors.forename: Chi-Hung
authors.initials: CH
authors.lastname: Huang
authors.forename: Chia-Shin
authors.initials: CS
authors.lastname: Yang
authors.forename: Chi-Huang
authors.initials: CH
authors.lastname: Chang
authors.forename: Shu-Min
authors.initials: SM
authors.lastname: Kuan
authors.forename: Nei-Li
authors.initials: NL
authors.lastname: Chan
authors.forename: Yeh
authors.initials: Y
authors.lastname: Chen
mesh_terms: D020134:Catalytic Domain; D003460:Crystallization; D034301:Deinococcus / Q000201:enzymology*; D015870:Gene Expression; D053484:RecQ Helicases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D014961:X-Ray Diffraction
chemical_list: D053484:RecQ Helicases