University of Illinois at Chicago
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Crystallization and preliminary X-ray characterization of the glpX-encoded class II fructose-1,6-bisphosphatase from Mycobacterium tuberculosis

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journal contribution
posted on 2012-03-09, 00:00 authored by Hiten J. Gutka, Scott G. Franzblau, Farahnaz Movahedzadeh, Celerino Abad-Zapatero
Fructose-1,6-bisphosphatase (FBPase; EC, 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 P6122, 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.


The authors are grateful to the American Lung Association (Grant No. RG-82534-N) for their support. Supporting institutions may be found at Use of the Advanced Photon Source was supported by the US Department of Energy, Office of Science, Office of Basic Energy Sciences under Contract No. W-31-109-Eng-38.


Publisher Statement

The original version is available through International Union of Crystallography at DOI: 10.1107/S1744309111014722.


International Union of Crystallography


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