Crystallization and preliminary X-ray characterization of a glycerol dehydrogenase from the human pathogen Salmonella enterica serovar Typhimurium

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Abstract

Glycerol dehydrogenase (GldA) encoded by the STM4108 gene (gldA) has been related to the synthesis of HilA, a major transcriptional regulator that is responsible for the expression of invasion genes in the human pathogen Salmonella enterica serovar Typhimurium. Single colourless crystals were obtained from a recombinant preparation of GldA overexpressed in Escherichia coli. They belonged to space group P222(1), with unit-cell parameters a = 127.0, b = 160.1, c = 665.2 angstrom. The crystals contained a very large number of molecules in the asymmetric unit, probably 30-35. Diffraction data were collected to 3.5 angstrom resolution using synchrotron radiation at the European Synchrotron Radiation Facility.
Original languageUnknown
Pages (from-to)698-701
JournalActa Crystallographica Section F-Structural Biology And Crystallization Com
Volume65
Issue numberNA
DOIs
Publication statusPublished - 1 Jan 2009

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