Overproduction, crystallization and preliminary X-ray analysis of the putative l-ascorbate-6-phosphate lactonase UlaG from Escherichia coli
- Structural Biology Department, Institut de Biologia Molecular de Barcelona and Institut de Recerca Biomèdica, E-08028 Barcelona (Spain)
- Department of Biochemistry, School of Pharmacy, University of Barcelona, Avenida Diagonal 643, E-08028 Barcelona (Spain)
UlaG, the putative l-ascorbate-6-phosphate lactonase encoded by the ulaG gene from the utilization of l-ascorbate regulon in E. coli, has been cloned, overexpressed, purified using standard chromatographic techniques and crystallized in a monoclinic space group. Crystals were obtained by the sitting-drop vapour-diffusion method at 293 K. A data set diffracting to 3 Å resolution was collected from a single crystal at 100 K. UlaG, 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 Å{sup 3} Da{sup −1} and a solvent content of 43%.
- OSTI ID:
- 22360469
- Journal Information:
- Acta Crystallographica. Section F, Vol. 64, Issue Pt 1; Other Information: PMCID: PMC2373999; PMID: 18097099; PUBLISHER-ID: ll5136; OAI: oai:pubmedcentral.nih.gov:2373999; Copyright (c) International Union of Crystallography 2008; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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