Crystallization And Preliminary X-Ray Diffraction Analysis Of Phosphoglucose Isomerase From Pyrococcus Furiosus

Title: Crystallization And Preliminary X-Ray Diffraction Analysis Of Phosphoglucose Isomerase From Pyrococcus Furiosus

Volume: 10 Issue: 5

Author(s): Michael K. Swan, Thomas Hansen, Peter Schonheit and Christopher Davies

Affiliation:

Keywords: pyrococcus furiosus, phosphoglucose isomerase, cupin fold, x-ray crystallography

Abstract: In several euryarchaeota, phosphoglucose isomerase (PGI) activity is catalyzed by an enzyme unrelated to the well-known family of PGI enzymes found in prokaryotes, eukaryotes and some archaea. In order to understand the mechanistic differences between the two families of enzymes we have crystallized PGI from the archaeon Pyrococcus furiosus. The crystals belong to the space group P21 and a complete dataset extending to 1.9 Å resolution has been collected.

Cite this article as:

Swan K. Michael, Hansen Thomas, Schonheit Peter and Davies Christopher, Crystallization And Preliminary X-Ray Diffraction Analysis Of Phosphoglucose Isomerase From Pyrococcus Furiosus, Protein & Peptide Letters 2003; 10 (5) . https://dx.doi.org/10.2174/0929866033478762