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

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 Angstrom, b=89.6 Angstrom and c=136.2 Angstrom. Under cryoconditions (120 K), a complete data set up to 2.8 Angstrom was collected at a synchrotron source. (C) 2004 Elsevier B.V. All rights reserved.