Open AccessPurification, crystallization and X‐ray diffraction analysis of pavine N ‐methyltransferase from Thalictrum flavum
Author(s) -
Jain Ankur,
Ziegler Jörg,
Liscombe David K.,
Facchini Peter J.,
Tucker Paul A.,
Panjikar Santosh
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108033046
Subject(s) - benzylisoquinoline , chemistry , methyltransferase , derivative (finance) , crystallization , size exclusion chromatography , complementary dna , enzyme , anomalous scattering , x ray crystallography , escherichia coli , crystallography , stereochemistry , biochemistry , diffraction , dna , biosynthesis , organic chemistry , methylation , physics , financial economics , economics , gene , optics
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 P 2 1 . The structure was solved at 2.0 Å resolution using a xenon derivative and the single isomorphous replacement with anomalous scattering method.