Acta Crystallographica Section D

Biological Crystallography

Volume 58, Part 9 (September 2002)

crystallization papers

Acta Cryst. (2002). D58, 1470-1473 [ doi:10.1107/S0907444902010685 ]

Crystallization and preliminary X-ray analysis of an R-2-hydroxypropyl-coenzyme M dehydrogenase

B. Nocek, D. D. Clark, S. A. Ensign and J. W. Peters

Abstract: The R-2-hydroxypropyl-coenzyme M (2-mercaptoethanesulfonate) dehydrogenase is a key enzyme in the microbial conversion of propylene to the central metabolite acetoacetate. This enzyme is an interesting member of the NAD(P)H-dependent short-chain dehydrogenase/reductase (SDR) family of enzymes, being one of a pair of homologous dehydrogenases that act in concert in a single pathway to convert the R- and S-enantiomers of hydroxypropyl-coenzyme M to the achiral ketopropyl-coenzyme M product. Crystallization trials have revealed that the highest diffraction quality crystals (better than 2.0 Å resolution) could be achieved when the reaction substrates were added to the enzyme in a stoichiometric excess prior to crystallization.

Keywords: R-2-hydroxypropyl-coenzyme M dehydrogenase.