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  • Title: Purification, crystallization and X-ray diffraction analysis of pavine N-methyltransferase from Thalictrum flavum.
    Author: Jain A, Ziegler J, Liscombe DK, Facchini PJ, Tucker PA, Panjikar S.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2008 Nov 01; 64(Pt 11):1066-9. PubMed ID: 18997344.
    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.
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