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  • Title: Crystallization and preliminary X-ray crystallographic analysis of strictosidine synthase from Rauvolfia: the first member of a novel enzyme family.
    Author: Ma X, Koepke J, Fritzsch G, Diem R, Kutchan TM, Michel H, Stöckigt J.
    Journal: Biochim Biophys Acta; 2004 Oct 01; 1702(1):121-4. PubMed ID: 15450856.
    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.
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