Crystallization and preliminary X-ray analysis of strictosidine synthase and its complex with the substrate
Juergen Koepke1, Xueyan Ma, Günter Fritzsch
1Department of Molecular Membrane Biology, Max-Planck-Institute of Biophysics, Marie-Curie-Strasse 15, D-60439 Frankfurt/Main, Germany.
Abstract:
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 A and have unit-cell parameters a = b = 150.3, c = 122.4 A. The tryptamine complex crystals diffract to 2.38 A, with unit-cell parameters a = b = 147.3, c = 122.3 A.
More Related Videos
11:27X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
10:45Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
Published on: March 20, 2021
Related Concept Videos
X-ray Diffraction of Biological Samples
According to Bragg's law, when X-rays strike the sample positioned on a stage, the rays are scattered by the electron clouds around the sample atoms. The X-ray diffraction or scattering is caused by constructive interference of the X-ray waves that reflect off the internal crystal...
Determination of Crystal Structures
