title: Heterologous expression, purification, crystallization and preliminary X-ray analysis of raucaffricine glucosidase, a plant enzyme specifically involved in Rauvolfia alkaloid biosynthesis.
abstract: Raucaffricine glucosidase (RG) is an enzyme that is specifically involved in the biosynthesis of indole alkaloids from the plant Rauvolfia serpentina. After heterologous expression in Escherichia coli cells, crystals of RG were obtained by the hanging-drop vapour-diffusion technique at 293 K with 0.3 M ammonium sulfate, 0.1 M sodium acetate pH 4.6 buffer and 11% PEG 4000 as precipitant. Crystals belong to space group I222 and diffract to 2.30 A, with unit-cell parameters a = 102.8, b = 127.3, c = 215.8 A.
authors.affiliation: Department of Pharmaceutical Biology, Institute of Pharmacy, Johannes Gutenberg-University Mainz, Staudinger Weg 5, D-55099 Mainz, Germany.
authors.forename: Martin
authors.initials: M
authors.lastname: Ruppert
authors.forename: Santosh
authors.initials: S
authors.lastname: Panjikar
authors.forename: Leif
authors.initials: L
authors.lastname: Barleben
authors.forename: Joachim
authors.initials: J
authors.lastname: Stöckigt
mesh_terms: D003001:Cloning, Molecular; D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D005959:Glucosidases / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D011926:Rauwolfia / Q000201:enzymology
chemical_list: D005959:Glucosidases; C119910:raucaffricine beta-glucosidase