Open AccessCrystallization and preliminary crystallographic studies of Mycobacterium tuberculosis DNA gyrase B C‐terminal domain, part of the enzyme reaction core
Author(s) -
Fu Guangsen,
Wu Jinjun,
Zhu Deyu,
Hu Yonglin,
Bi Lijun,
Zhang XianEn,
Wang DaCheng
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109006575
Subject(s) - crystallization , dna gyrase , crystallography , core (optical fiber) , domain (mathematical analysis) , terminal (telecommunication) , mycobacterium tuberculosis , enzyme , materials science , chemistry , tuberculosis , biochemistry , escherichia coli , medicine , organic chemistry , pathology , gene , mathematical analysis , telecommunications , mathematics , computer science , composite material
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 Å, respectively. These crystals belonged to space group P 2 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 Å.