Purification, crystallization and preliminary crytallographic analysis of phosphoglucose isomerase from the hyperthermophilic archaeon Pyrococcus furiosus

A.P. Akerboom, A.P. Turnbull, D. Hargreaves, M. Fischer, D. de Geus, S.E. Sedelnikova, J.M. Berrisford, P.J. Baker, C.H. Verhees, J. van der Oost, D.W. Rice

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Abstract

The glycolytic enzyme phosphoglucose isomerase catalyses the reversible isomerization of glucose 6-phosphate to fructose 6-phosphate. The phosphoglucose isomerase from the hyperthermophilic archaeon Pyrococcus furiosus, which shows no sequence similarity to any known bacterial or eukaryotic phosphoglucose isomerase, has been cloned and overexpressed in Escherichia coli, purified and subsequently crystallized by the hanging-drop method of vapour diffusion using 1.6 M sodium citrate as the precipitant at pH 6.5. Multiple-wavelength anomalous dispersive X-ray data have been collected to a maximum resolution of 1.92 Angstrom on a single selenomethionine-incorporated crystal. This crystal belongs to space group C2, with approximate unit-cell parameters a = 84.7, b= 42.4, c= 57.3 Angstrom, beta = 120.6degrees and a monomer in the asymmetric unit.
Original languageEnglish
Pages (from-to)1822-1823
JournalActa Crystallographica Section D-Biological Crystallography
Volume59
DOIs
Publication statusPublished - 2003

Keywords

  • cupin superfamily
  • crystal-structure
  • mechanism
  • protein

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