title: Crystallization and preliminary crystallographic studies of UbiG, an O-methyltransferase from Escherichia coli.
abstract: 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 C121, 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)).
authors.affiliation: School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui, People's Republic of China.
authors.forename: Li
authors.initials: L
authors.lastname: Xing
authors.forename: Yuwei
authors.initials: Y
authors.lastname: Zhu
authors.forename: Pengfei
authors.initials: P
authors.lastname: Fang
authors.forename: Jing
authors.initials: J
authors.lastname: Wang
authors.forename: Fuxing
authors.initials: F
authors.lastname: Zeng
authors.forename: Xuesong
authors.initials: X
authors.lastname: Li
authors.forename: Maikun
authors.initials: M
authors.lastname: Teng
authors.forename: Xu
authors.initials: X
authors.lastname: Li
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D008780:Methyltransferases / Q000737:chemistry*
chemical_list: D029968:Escherichia coli Proteins; D008780:Methyltransferases; C019616:UbiG protein, E coli