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Crystallization and preliminary X-ray characterization of a glycerol dehydrogenase from the human pathogen Salmonella enterica serovar Typhimurium
DOI: 10.1107/S1744309109020296
International Union of Crystallography, 2009
Additional Information
How to Cite
Gonçalves, A. T., Marçal, D., Carrondo, M. A. and Enguita, F. J. (2009), Crystallization and preliminary X-ray characterization of a glycerol dehydrogenase from the human pathogen Salmonella enterica serovar Typhimurium. Acta Cryst. F, 65: 698–701. doi: 10.1107/S1744309109020296
Keywords:
- glycerol dehydrogenase;
- Salmonella enterica serovar Typhimurium;
- family III alcohol dehydrogenases;
- foodborne infections
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 P2221, with unit-cell parameters a = 127.0, b = 160.1, c = 665.2 Å. The crystals contained a very large number of molecules in the asymmetric unit, probably 30–35. Diffraction data were collected to 3.5 Å resolution using synchrotron radiation at the European Synchrotron Radiation Facility.