title: Crystallization and preliminary crystallographic studies of Mycobacterium tuberculosis DNA gyrase B C-terminal domain, part of the enzyme reaction core.
abstract: DNA gyrase subunit B C-terminal domain (GyrB-CTD) is a functional module of DNA gyrase which participates in forming the core of DNA gyrase and plays critical roles in G-segment binding and T-segment loading and passage. Here, the purification, crystallization and preliminary X-ray crystallographic studies of GyrB-CTD from Mycobacterium tuberculosis H37Rv are reported. Diffraction data were collected from crystals of native GyrB-CTD and its selenomethionine derivative to resolutions of 2.8 and 3.0 A, respectively. These crystals belonged to space group P2(1)2(1)2(1) with similar unit-cell parameters. The native protein crystals had unit-cell parameters a = 52.831, b = 52.763, c = 192.579 A.
authors.affiliation: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
authors.forename: Guangsen
authors.initials: G
authors.lastname: Fu
authors.forename: Jinjun
authors.initials: J
authors.lastname: Wu
authors.forename: Deyu
authors.initials: D
authors.lastname: Zhu
authors.forename: Yonglin
authors.initials: Y
authors.lastname: Hu
authors.forename: Lijun
authors.initials: L
authors.lastname: Bi
authors.forename: Xian En
authors.initials: XE
authors.lastname: Zhang
authors.forename: Da Cheng
authors.initials: da C
authors.lastname: Wang