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 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 A. The crystals contained a very large number of molecules in the asymmetric unit, probably 30-35. Diffraction data were collected to 3.5 A resolution using synchrotron radiation at the European Synchrotron Radiation Facility.
Gonçalves
A T
AT
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 2781-901 Oeiras, Portugal.
Marçal
D
D
Carrondo
M A
MA
Enguita
F J
FJ
D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D019779:Salmonella enterica / Q000201:enzymology*; D013401:Sugar Alcohol Dehydrogenases / Q000737:chemistry*
D013401:Sugar Alcohol Dehydrogenases; C020672:glycerol dehydrogenase