Abstract
Mevalonate diphosphate decarboxylase catalyses the last and least well characterized step in the mevalonate pathway for the biosynthesis of isopentenyl pyrophosphate, an isoprenoid precursor. A gene predicted to encode the enzyme from Trypanosoma brucei has been cloned, a highly efficient expression system established and a purification protocol determined. The enzyme gives monoclinic crystals in space group P2(1), with unit-cell parameters a = 51.5, b = 168.7, c = 54.9 A, beta = 118.8 degrees. A Matthews coefficient VM of 2.5 A3 Da(-1) corresponds to two monomers, each approximately 42 kDa (385 residues), in the asymmetric unit with 50% solvent content. These crystals are well ordered and data to high resolution have been recorded using synchrotron radiation.
Original language | English |
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Pages (from-to) | 581-4 |
Number of pages | 4 |
Journal | Acta Crystallographica F-Structural Biology and Crystallization Communications |
Volume | 61 |
Issue number | Pt 6 |
DOIs | |
Publication status | Published - 1 Jun 2005 |
Keywords
- Animals
- Carboxy-Lyases/chemistry
- Cloning, Molecular
- Crystallization
- Protozoan Proteins/chemistry
- Trypanosoma brucei brucei/enzymology
- X-Ray Diffraction