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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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 A resolution) could be achieved when the reaction substrates were added to the enzyme in a stoichiometric excess prior to crystallization.[1]

References

  1. Crystallization and preliminary X-ray analysis of an R-2-hydroxypropyl-coenzyme M dehydrogenase. Nocek, B., Clark, D.D., Ensign, S.A., Peters, J.W. Acta Crystallogr. D Biol. Crystallogr. (2002) [Pubmed]
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