Purification, crystallization and X-ray diffraction analysis of pavineN-methyltransferase fromThalictrum flavum Academic Article uri icon

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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.

authors

  • Jain, Ankur
  • Ziegler, Jörg
  • Liscombe, David
  • Facchini, Peter J
  • Tucker, Paul A
  • Panjikar, Santosh

publication date

  • November 1, 2008