Open AccessCrystallization and preliminary X‐ray diffraction analysis of mevalonate kinase from Methanosarcina mazei
Author(s) -
Zhuang Ningning,
Seo Kyung Hye,
Chen Cong,
Zhou Jia,
Kim Seon Won,
Lee Kon Ho
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112047070
Subject(s) - methanosarcina , crystallization , mevalonate pathway , crystallography , chemistry , biosynthesis , methanosarcina barkeri , biochemistry , stereochemistry , enzyme , archaea , gene , organic chemistry , methanogenesis , methane
Mevalonate kinase (MVK), which plays an important role in catalysing the biosynthesis of isoprenoid compounds derived from the mevalonate pathway, transforms mevalonate to 5‐phosphomevalonate using ATP as a cofactor. Mevalonate kinase from Methanosarcina mazei ( Mm MVK) was expressed in Escherichia coli , purified and crystallized for structural analysis. Diffraction‐quality crystals of Mm MVK were obtained by the vapour‐diffusion method using 0.32 M MgCl 2 , 0.08 M bis‐tris pH 5.5, 16%( w / v ) PEG 3350. The crystals belonged to space group P 2 1 2 1 2, with unit‐cell parameters a = 97.11, b = 135.92, c = 46.03 Å. Diffraction data were collected to 2.08 Å resolution.