Purification, crystallization and X-ray diffraction analysis of pavineN-methyltransferase fromThalictrum flavum
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A cDNA from the plant Thalictrum flavum encoding pavine N-methyltransferase, an enzyme belonging to a novel class of S-adenosylmethionine-dependent N-methyltransferases specific for benzylisoquinoline alkaloids, has been heterologously expressed in Escherichia coli. The enzyme was purified using affinity and gel-filtration chromatography and was crystallized in space group P2(1). The structure was solved at 2.0 A resolution using a xenon derivative and the single isomorphous replacement with anomalous scattering method.
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