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

6533b830fe1ef96bd12971c3

RESEARCH PRODUCT

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

Hartmut Michel Ralf Diem Toni M. Kutchan Juergen Koepke Joachim Stöckigt Günter Fritzsch Xueyan Ma

subject

Rauvolfia Strictosidine synthase DNA Plant Stereochemistry Biophysics medicine.disease_cause Crystallography X-Ray Biochemistry Rauwolfia Analytical Chemistry law.invention chemistry.chemical_compound Biosynthesis law Rauvolfia serpentina Carbon-Nitrogen Lyases medicine Escherichia coli Crystallization Molecular Biology Escherichia coli chemistry.chemical_classification Tetrahydrate biology Base Sequence biology.organism_classification Recombinant Proteins Enzyme chemistry Biochemistry biology.protein

description

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.

year	journal	country	edition	language
2004-04-27	Biochimica et biophysica acta

10.1016/j.bbapap.2004.06.013 https://pubmed.ncbi.nlm.nih.gov/15450856

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