crystallization.pdf (304.69 kB)
Crystallization and preliminary X-ray characterization of the glpX-encoded class II fructose-1,6-bisphosphatase from Mycobacterium tuberculosis
journal contributionposted 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 22.214.171.124), 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 http://www.ser-cat.org/members.html. 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 StatementThe original version is available through International Union of Crystallography at DOI: 10.1107/S1744309111014722.
PublisherInternational Union of Crystallography