ISSN:
1399-0047
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Chemistry and Pharmacology
,
Geosciences
,
Physics
Notes:
Encoded by the agp gene, Escherichia coli glucose-1-phosphatase hydrolyzes glucose-1-phosphate in the periplasmic space of the bacterium. It is a potential drug-design target because inositol phosphatases have been identified as important virulence determinants in several human and animal pathogens. The enzyme was isolated and purified to homogeneity from a strain of E. coli CU1867 (an appA-deficient mutant). Crystals were obtained overnight by the equilibrium vapour-diffusion method from a solution containing 10 mg ml−1 enzyme, 1.2 M ammonium sulfate and 25% polyethylene glycol monomethyl ether 5000 in 0.1 M MES at pH 6.5. The crystals belong to space group R3, with unit-cell parameters a = b = 156.0, c = 92.2 Å. The diffraction limit was 2.6 Å at a rotating-anode X-ray source; a 2.7 Å resolution data set has been collected using light mineral oil as a cryoprotectant. The data set was 95.2% complete, with an Rsym of 0.058. There were two monomers of glucose-1-phosphatase in the asymmetric unit, which correspond to a VM of 2.36 Å Da−1 and 47.5% solvent content. Self-rotation analysis unambiguously shows a twofold non-crystallographic symmetry.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S090744490001979X
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