Vinorine synthase from Rauvolfia: the first example of crystallization and preliminary X-ray diffraction analysis of an enzyme of the BAHD superfamily

Biochim Biophys Acta. 2004 Sep 1;1701(1-2):129-32. doi: 10.1016/j.bbapap.2004.06.011.


Crystals of vinorine synthase (VS) from medicinal plant Rauvolfia serpentina expressed in Escherichia coli have been obtained by the hanging-drop technique at 305 K with ammonium sulfate and PEG 400 as precipitants. The enzyme is involved in the biosynthesis of the antiarrhythmic drug ajmaline and is a member of the BAHD superfamily of acyltransferases. So far, no three-dimensional structure of a member of this enzyme family is known. The crystals belong to the space group P2(1)2(1)2(1) with cell dimensions of a=82.3 A, b=89.6 A and c=136.2 A. Under cryoconditions (120 K), a complete data set up to 2.8 A was collected at a synchrotron source.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkaloids / metabolism
  • Crystallization
  • Crystallography, X-Ray
  • Enzymes / chemistry
  • Enzymes / isolation & purification*
  • Indoles / metabolism
  • Rauwolfia / enzymology*


  • Alkaloids
  • Enzymes
  • Indoles
  • vellosimine