title: Crystallization and preliminary X-ray diffraction analysis of phosphoglucose isomerase from Pyrococcus furiosus.
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 P2(1) and a complete dataset extending to 1.9 A resolution has been collected.
authors.affiliation: Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, South Carolina 29425, USA.
authors.forename: Michael K
authors.initials: MK
authors.lastname: Swan
authors.forename: Thomas
authors.initials: T
authors.lastname: Hansen
authors.forename: Peter
authors.initials: P
authors.lastname: Schönheit
authors.forename: Christopher
authors.initials: C
authors.lastname: Davies
mesh_terms: D003460:Crystallization; D005956:Glucose-6-Phosphate Isomerase / Q000737:chemistry* / Q000302:isolation & purification; D020027:Pyrococcus furiosus / Q000201:enzymology*; D014961:X-Ray Diffraction / Q000706:statistics & numerical data
chemical_list: D005956:Glucose-6-Phosphate Isomerase