Open AccessOverproduction, crystallization and preliminary X‐ray analysis of the putative l ‐ascorbate‐6‐phosphate lactonase UlaG from Escherichia coli
Author(s) -
Garces Fernando,
Fernández Francisco J.,
PérezLuque Rosa,
Aguilar Juan,
Baldomà Laura,
Coll Miquel,
Badía Josefa,
Vega M. Cristina
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107065256
Subject(s) - escherichia coli , monoclinic crystal system , chemistry , crystallization , phosphate , biochemistry , microbiology and biotechnology , crystallography , biology , gene , crystal structure , organic chemistry
UlaG, the putative l ‐ascorbate‐6‐phosphate lactonase encoded by the ula G gene from the utilization of l ‐ascorbate regulon in Escherichia coli , has been cloned, overexpressed, purified using standard chromatographic techniques and crystallized. Crystals were obtained by sitting‐drop vapour diffusion at 293 K. Preliminary X‐ray diffraction analysis revealed that the UlaG crystals belonged to the monoclinic space group C 2, with unit‐cell parameters a = 104.52, b = 180.69, c = 112.88 Å, β = 103.26°. The asymmetric unit is expected to contain six copies of UlaG, with a corresponding volume per protein weight of 2.16 Å 3 Da −1 and a solvent content of 43%.