Open AccessCrystallization and preliminary X‐ray crystallographic studies of O ‐methyltransferase from Anabaena PCC 7120
Author(s) -
Li Guoming,
Tang Zhenting,
Meng Geng,
Dai Kesheng,
Zhao Jindong,
Zheng Xiaofeng
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109035118
Subject(s) - crystallization , anabaena , escherichia coli , chemistry , bacteria , stereochemistry , crystallography , recombinant dna , enzyme , molecule , methyltransferase , biochemistry , methylation , biology , cyanobacteria , organic chemistry , dna , gene , genetics
O ‐Methyltransferase (OMT) is a ubiquitous enzyme that exists in bacteria, plants and humans and catalyzes a methyl‐transfer reaction using S ‐adenosyl‐ l ‐methionine as a methyl donor and a wide range of phenolics as acceptors. To investigate the structure and function of OMTs, omt from Anabaena PCC 7120 was cloned into expression vector pET21a and expressed in a soluble form in Escherichia coli strain BL21 (DE3). The recombinant OMT protein was purified to homogeneity using a two‐step strategy. Crystals of OMT that diffracted to a resolution of 2.4 Å were obtained using the hanging‐drop vapour‐diffusion method. The crystals belonged to space group C 222 1 , with unit‐cell parameters a = 131.620, b = 227.994, c = 150.777 Å, α = β = γ = 90°. There are eight molecules per asymmetric unit.