A preliminary crystallographic analysis of the putative mevalonate diphosphate decarboxylase from Trypanosoma brucei

Research output: Contribution to journalArticle

3 Citations (Scopus)

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 languageEnglish
Pages (from-to)581-4
Number of pages4
JournalActa Crystallographica F-Structural Biology and Crystallization Communications
Volume61
Issue numberPt 6
DOIs
Publication statusPublished - 1 Jun 2005

Keywords

  • Animals
  • Carboxy-Lyases/chemistry
  • Cloning, Molecular
  • Crystallization
  • Protozoan Proteins/chemistry
  • Trypanosoma brucei brucei/enzymology
  • X-Ray Diffraction

Fingerprint Dive into the research topics of 'A preliminary crystallographic analysis of the putative mevalonate diphosphate decarboxylase from Trypanosoma brucei'. Together they form a unique fingerprint.

  • Cite this