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

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INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309110001740

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Funding

  1. Protein 3000 Project
  2. MEXT of Japan

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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 angstrom 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 angstrom. Structural analysis by molecular replacement is in progress.

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