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

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Koepke,  Jürgen
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Linhard,  Verena
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Fritzsch,  Günter
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Michel,  Hartmut
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Ma, X., Koepke, J., Bayer, A., Linhard, V., Fritzsch, G., Zhang, B., et al. (2004). Vinorine synthase from Rauvolfia: the first example of crystallization and preliminary X-ray diffraction analysis of an enzyme of the BAHD superfamily. Biochimica et Biophysica Acta-Proteins and Proteomics, 1701(1-2), 129-132. doi:10.1016/j.bbapap.2004.06.011.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-DAC7-D
Abstract
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 P212121 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.