title: Crystallization and preliminary X-ray characterization of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv.
abstract: Phosphoglucose isomerase is a ubiquitous enzyme that catalyzes the isomerization of D-glucopyranose-6-phosphate to D-fructofuranose-6-phosphate. The present investigation reports the expression, purification, crystallization and preliminary crystallographic studies of the phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv, which shares 46% sequence identity with that of its human host. The recombinant protein, which was prepared using an Escherichia coli expression system, was crystallized by the hanging-drop vapour-diffusion method. The crystals diffracted to a resolution of 2.8 A and belonged to the orthorhombic space group I2(1)2(1)2(1), with unit-cell parameters a = 109.0, b = 119.8, c = 138.9 A.
authors.affiliation: Gene Regulation Laboratory, National Institute of Immunology, New Delhi 110067, India.
authors.forename: Divya
authors.initials: D
authors.lastname: Mathur
authors.forename: Kanchan
authors.initials: K
authors.lastname: Anand
authors.forename: Deepika
authors.initials: D
authors.lastname: Mathur
authors.forename: Nirmala
authors.initials: N
authors.lastname: Jagadish
authors.forename: Anil
authors.initials: A
authors.lastname: Suri
authors.forename: Lalit C
authors.initials: LC
authors.lastname: Garg
mesh_terms: D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D005956:Glucose-6-Phosphate Isomerase / Q000737:chemistry* / Q000302:isolation & purification; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D011487:Protein Conformation
chemical_list: D005956:Glucose-6-Phosphate Isomerase