Crystallization and preliminary X-ray diffraction analysis of phosphoglucose isomerase from Pyrococcus furiosus.
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.
Swan
Michael K
MK
Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, South Carolina 29425, USA.
Hansen
Thomas
T
Schönheit
Peter
P
Davies
Christopher
C
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
D005956:Glucose-6-Phosphate Isomerase