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O-Methyltransferases (OMTs), one of the ubiquitousenzymes in plants, bacteria, and humans, catalyze a methyl-transfer reaction using S-adenosylmethionine and a wide rangeof phenolics as a methyl donor and aceptor, respectively.Substrates for most bacterial OMTs have largely remainedelusive, but recent investigation using BcOMT2, an OMT fromBacillus cereus, suggested that ortho-dihydroxyflavonoids couldserve as substrates. To elucidate the functional and structuralfeatures of BcOMT2, we expresed, and purified BcOMT2,and crystallized an apoenzyme and its ternary complexin the presence of a flavonoid and S-adenosylhomocysteine.Each crystal diffracted to 1.8 with its space group of C2and P212121and its ternary complex will provide the structural basisof methyl transfer onto (iso)flavonoids in a regiospecificmaner.