6533b81ffe1ef96bd1278575
RESEARCH PRODUCT
Heterologous expression, purification, crystallization and preliminary X-ray analysis of raucaffricine glucosidase, a plant enzyme specifically involved in Rauvolfia alkaloid biosynthesis
Santosh PanjikarMartin RuppertJoachim StöckigtJoachim StöckigtLeif Barlebensubject
RauvolfiaStereochemistryBiophysicsmedicine.disease_causeCrystallography X-RayBiochemistryRauwolfiachemistry.chemical_compoundBiosynthesisStructural BiologyRauvolfia serpentinaGeneticsmedicineEscherichia coliCloning MolecularEscherichia colichemistry.chemical_classificationIndole testbiologyCondensed Matter Physicsbiology.organism_classificationEnzymechemistryBiochemistryCrystallization Communicationsbiology.proteinHeterologous expressionCrystallizationGlucosidasesGlucosidasesdescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2006-02-24 |