Crystallization and preliminary X-ray characterization of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv.
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.
Mathur
Divya
D
Gene Regulation Laboratory, National Institute of Immunology, New Delhi 110067, India.
Anand
Kanchan
K
Mathur
Deepika
D
Jagadish
Nirmala
N
Suri
Anil
A
Garg
Lalit C
LC
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
D005956:Glucose-6-Phosphate Isomerase