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Crystallization and preliminary X-ray crystallographic studies of O-methyltransferase from Anabaena PCC 7120.

ABSTRACT: 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.

SUBMITTER: Li G

PROVIDER: S-EPMC2765896 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray crystallographic studies of O-methyltransferase from Anabaena PCC 7120.

Li Guoming G Tang Zhenting Z Meng Geng G Dai Kesheng K Zhao Jindong J Zheng Xiaofeng X

Acta crystallographica. Section F, Structural biology and crystallization communications 20090925 Pt 10

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. Cr ...[more]

PMID: 19851017

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