Crystallization and preliminary X-ray analysis of native and selenomethionyl vinorine synthase from Rauvolfia serpentina
Acta Crystallographica Section D
Volume 61, Issue 6, pages 694–696, June 2005
How to Cite
Ma, X., Koepke, J., Bayer, A., Fritzsch, G., Michel, H. and Stöckigt, J. (2005), Crystallization and preliminary X-ray analysis of native and selenomethionyl vinorine synthase from Rauvolfia serpentina. Acta Crystallographica D, 61: 694–696. doi: 10.1107/S0907444904028756
- vinorine synthase;
- ajmaline biosynthesis.
Vinorine synthase (VS) is a central enzyme of the biosynthesis of the antiarrhythmic drug ajmaline and is a member of the BAHD superfamily of acyltransferases. So far, no three-dimensional structure with significant sequence homology with VS is known. Crystals of VS and selenomethionyl-labelled VS from the medicinal plant Rauvolfia serpentina have been obtained by the hanging-drop technique at 305 K with ammonium sulfate and PEG 400 as precipitants. VS crystals diffract to 2.8 Å and belong to space group P212121, with unit-cell parameters a = 82.3, b = 89.6, c = 136.2 Å. The selenomethionyl VS crystal was nearly isomorphous with the VS crystal.