Open AccessHeterologous expression, purification, crystallization and preliminary X‐ray analysis of raucaffricine glucosidase, a plant enzyme specifically involved in Rauvolfia alkaloid biosynthesis
Author(s) -
Ruppert Martin,
Panjikar Santosh,
Barleben Leif,
Stöckigt Joachim
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910600457x
Subject(s) - biosynthesis , alkaloid , enzyme , heterologous expression , heterologous , crystallization , biochemistry , chemistry , stereochemistry , biology , organic chemistry , recombinant dna , gene
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 I 222 and diffract to 2.30 Å, with unit‐cell parameters a = 102.8, b = 127.3, c = 215.8 Å.