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Overproduction, crystallization and preliminary X-ray analysis of the putative L-ascorbate-6-phosphate lactonase UlaG from Escherichia coli

AuthorsGarces, Fernando ; Fernández, Francisco J. ; Pérez-Luque, Rosa ; Aguilar, Juan; Baldomá, Laura; Coll, Miquel ; Badía, Josefa; Vega, María Cristina
l-ascorbate metabolism
enterobacterial metabolism
Issue Date2008
CitationActa Crystallographica Section F 64(1):36-38(2008)
AbstractUlaG, the putative l-ascorbate-6-phosphate lactonase encoded by the ulaG 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 C2, 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 Å3 Da−1 and a solvent content of 43%
Description3 páginas, 3 figuras, 1 tabla -- PGS nros. 36-38
Publisher version (URL)http://dx.doi.org/0.1107/S1744309107065256
Appears in Collections:(CIB) Artículos
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