Crystallization and preliminary X-ray crystallographic analysis of 
strictosidine synthase from Rauvolfia: the first member of a novel enzyme family

Ma, Xueyan; Koepke, Jürgen; Fritzsch, Günter; Diem, Ralf; Kutchan, Toni M.; Michel, Hartmut; Stöckigt, Joachim

doi:10.1016/j.bbapap.2004.06.013

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Crystallization and preliminary X-ray crystallographic analysis of strictosidine synthase from Rauvolfia: the first member of a novel enzyme family

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Koepke, Jürgen
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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Diem, Ralf
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., Fritzsch, G., Diem, R., Kutchan, T. M., Michel, H., et al. (2004). Crystallization and preliminary X-ray crystallographic analysis of strictosidine synthase from Rauvolfia: the first member of a novel enzyme family. Biochimica et Biophysica Acta-Proteins and Proteomics, 1702, 121-124. doi:10.1016/j.bbapap.2004.06.013.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-DACA-7

Abstract

Strictosidine synthase is a central enzyme involved in the biosynthesis of almost all plant monoterpenoid indole alkaloids. Strictosidine synthase from Rauvolfia serpentina was heterologously expressed in Escherichia coli. Crystals of the purified recombinant enzyme have been obtained by the hanging-drop technique at 303 K with potassium sodium tartrate tetrahydrate as precipitant. The crystals belong to the space group R3 with cell dimensions of a=b=150.3 A and c=122.4 A. Under cryoconditions (120 K), the crystals diffract to about 2.95 A.