title: Crystallization and preliminary X-ray characterization of the glpX-encoded class II fructose-1,6-bisphosphatase from Mycobacterium tuberculosis.
abstract: Fructose-1,6-bisphosphatase (FBPase; EC 3.1.3.11), which is a key enzyme in gluconeogenesis, catalyzes the hydrolysis of fructose 1,6-bisphosphate to form fructose 6-phosphate and orthophosphate. The present investigation reports the crystallization and preliminary crystallographic studies of the glpX-encoded class II FBPase from Mycobacterium tuberculosis H37Rv. The recombinant protein, which was cloned using an Escherichia coli expression system, was purified and crystallized using the hanging-drop vapor-diffusion method. The crystals diffracted to a resolution of 2.7 Å and belonged to the hexagonal space group P6(1)22, with unit-cell parameters a = b = 131.3, c = 143.2 Å. The structure has been solved by molecular replacement and is currently undergoing refinement.
authors.affiliation: Institute for Tuberculosis Research, University of Illinois at Chicago, Chicago, IL 60607, USA.
authors.forename: Hiten J
authors.initials: HJ
authors.lastname: Gutka
authors.forename: Scott G
authors.initials: SG
authors.lastname: Franzblau
authors.forename: Farahnaz
authors.initials: F
authors.lastname: Movahedzadeh
authors.forename: Cele
authors.initials: C
authors.lastname: Abad-Zapatero
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D005635:Fructosediphosphates / Q000737:chemistry* / Q000302:isolation & purification; D009169:Mycobacterium tuberculosis / Q000201:enzymology*
chemical_list: D005635:Fructosediphosphates; C029063:fructose-1,6-diphosphate