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 P2(1), with unit-cell parameters a = 91.9, b = 226.6, c = 232.6 A, beta = 92.9 degrees. The crystals probably contain two decamers in the asymmetric unit, with a V(M) value of 3.07 A3 Da(-1) and an estimated solvent content of 59%. Diffraction data were collected to 2.7 A resolution using synchrotron radiation at the ID14-4 beamline of the European Synchrotron Radiation Facility.

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Marçal, D., Rego, A. T., Fogg, M. J., Wilson, K. S., Carrondo, M. A., & Enguita, F. J. (2007). Crystallization and preliminary X-ray characterization of 1,3-propanediol dehydrogenase from the human pathogen Klebsiella pneumoniae. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 63(3), 249–251. https://doi.org/10.1107/S1744309107008834

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