6533b856fe1ef96bd12b27fa
RESEARCH PRODUCT
Crystallization and preliminary X-ray analysis of strictosidine synthase and its complex with the substrate tryptamine
Juergen KoepkeJoachim StöckigtXueyan MaHartmut MichelGünter Fritzschsubject
TryptamineStrictosidine synthaseTetrahydratebiologyStereochemistryPotassium sodium tartrateSubstrate (chemistry)General MedicineRauwolfiaTryptamineslaw.inventionchemistry.chemical_compoundchemistryBiosynthesisStructural BiologylawCarbon-Nitrogen Lyasesbiology.proteinHeterologous expressionCrystallizationCrystallizationPlant Proteinsdescription
Strictosidine synthase (STR1) is a central enzyme that participates in the biosynthesis of almost all plant monoterpenoid indole alkaloids. After heterologous expression in Escherichia coli, crystals of STR1 and its substrate complex with tryptamine were obtained by the hanging-drop technique at 302–304 K with potassium sodium tartrate tetrahydrate as precipitant. All crystals belong to space group R3. The native STR1 crystals diffract to 2.95 Å and have unit-cell parameters a = b = 150.3, c = 122.4 Å. The tryptamine complex crystals diffract to 2.38 Å, with unit-cell parameters a = b = 147.3, c = 122.3 Å.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2005-05-26 | Acta Crystallographica Section D Biological Crystallography |