Crystallization and preliminary X-ray characterization of a glycerol dehydrogenase from the human pathogen Salmonella enterica serovar Typhimurium
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 obtain...
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Veröffentlicht in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2009-07, Vol.65 (7), p.698-701 |
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Sprache: | eng |
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Zusammenfassung: | 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. |
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ISSN: | 1744-3091 1744-3091 |
DOI: | 10.1107/S1744309109020296 |