Crystallization and preliminary X-ray crystallographic study of phosphoglucose isomerase from Plasmodium falciparum

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Mar 1;66(Pt 3):333-6. doi: 10.1107/S1744309110001740. Epub 2010 Feb 25.

Abstract

Phosphoglucose isomerase (PGI) is a key enzyme in glycolysis and glycogenesis that catalyses the interconversion of glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P). For crystallographic studies, PGI from the human malaria parasite Plasmodium falciparum (PfPGI) was overproduced in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data to 1.5 A resolution were collected from an orthorhombic crystal form belonging to space group P2(1)2(1)2(1) with unit-cell parameters a = 103.3, b = 104.1, c = 114.6 A. Structural analysis by molecular replacement is in progress.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Glucose-6-Phosphate Isomerase / chemistry*
  • Glucose-6-Phosphate Isomerase / isolation & purification
  • Plasmodium falciparum / enzymology*

Substances

  • Glucose-6-Phosphate Isomerase