Open AccessCrystallization and preliminary crystallographic studies of UbiG, an O ‐methyltransferase from Escherichia coli
Author(s) -
Xing Li,
Zhu Yuwei,
Fang Pengfei,
Wang Jing,
Zeng Fuxing,
Li Xuesong,
Teng Maikun,
Li Xu
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111014278
Subject(s) - crystallization , escherichia coli , methyltransferase , crystallography , biosynthesis , chemistry , crystal structure , enzyme , molecule , solvent , stereochemistry , crystal (programming language) , methylation , biochemistry , dna , organic chemistry , gene , computer science , programming language
UbiG, an O ‐methyltransferase from the ubiquinone‐biosynthesis pathway in Escherichia coli , catalyzes two O ‐methyl transfer steps. The primary structures of the O ‐methyltransferase enzyme family used in ubiquinone synthesis are conserved in both prokaryotes and eukaryotes, but their tertiary structures and catalytic mechanisms are not yet known. Here, UbiG with an N‐terminal hexahistidine tag was expressed and crystallized. Crystals grown by the hanging‐drop vapour‐diffusion method diffracted to 2.00 Å resolution and belonged to space group C 121, with unit‐cell parameters a = 119.8, b = 58.6, c = 40.2 Å, β = 105.3°. Both Matthews coefficient analysis and the self‐rotation function suggested the presence of one molecule per asymmetric unit in the crystal, with a solvent content of 50.52% ( V M = 2.48 Å 3 Da −1 ).