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Purification, crystallization and X-ray diffraction analysis of pavine N-methyltransferase from Thalictrum flavum.

ABSTRACT: 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.

SUBMITTER: Jain A

PROVIDER: S-EPMC2581683 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature

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Purification, crystallization and X-ray diffraction analysis of pavine N-methyltransferase from Thalictrum flavum.

Jain Ankur A Ziegler Jörg J Liscombe David K DK Facchini Peter J PJ Tucker Paul A PA Panjikar Santosh S

Acta crystallographica. Section F, Structural biology and crystallization communications 20081031 Pt 11

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 ano ...[more]

PMID: 18997344

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