Crystallization and preliminary X-ray characterization of 1,3-propanediol dehydrogenase from the human pathogen Klebsiella pneumoniae

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Abstract

1,3-Propanediol dehydrogenase (1,3-PD-DH), encoded by the dhaT gene, is a key enzyme in the dissimilation process for converting glycerol to 1,3-propanediol in the human pathogen Klebsiella pneumoniae. Single colourless crystals were obtained from a recombinant preparation of 1,3- propanediol dehydrogenase overexpressed in Escherichia coli. The crystals belong to space group P21, with unit-cell parameters a = 91.9, b = 226.6, c = 232.6 angstrom, beta = 92.9 degrees. The crystals probably contain two decamers in the asymmetric unit, with a V-M value of 3.07 angstrom(3) Da(-1) and an estimated solvent content of 59%. Diffraction data were collected to 2.7 angstrom resolution using synchrotron radiation at the ID14- 4 beamline of the European Synchrotron Radiation Facility.
Original languageUnknown
Pages (from-to)249-251
JournalActa Crystallographica Section F-Structural Biology And Crystallization Com
Volume63
Issue numberNA
DOIs
Publication statusPublished - 1 Jan 2007

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