ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009
Crystallization and preliminary X-ray crystallographic studies of O-methyltransferase from Anabaena PCC 7120.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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.
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