Crystallization and preliminary X-ray crystallographic studies of O-methyltransferase from Anabaena PCC 7120.
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 A were obtained using the hanging-drop vapour-diffusion method. The crystals belonged to space group C222(1), with unit-cell parameters a = 131.620, b = 227.994, c = 150.777 A, alpha = beta = gamma = 90 degrees . There are eight molecules per asymmetric unit.
Li
Guoming
G
National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing 100871, People's Republic of China.
Tang
Zhenting
Z
Meng
Geng
G
Dai
Kesheng
K
Zhao
Jindong
J
Zheng
Xiaofeng
X
D017033:Anabaena / Q000201:enzymology*; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D008780:Methyltransferases / Q000737:chemistry* / Q000302:isolation & purification
D008780:Methyltransferases