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1: Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1732-4. Epub 2001 Oct 25.Click here to read Links

Crystallization of quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni: crystals with unique optical properties.

Oubrie A, Huizinga EG, Rozeboom HJ, Kalk KH, de Jong GA, Duine JA, Dijkstra BW.

Laboratory of Biophysical Chemistry and BIOSON Research Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.

Quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni is a functional electron-transfer protein containing both a haem c and a pyrroloquinoline quinone cofactor. The enzyme has been crystallized at 277 K using polyethylene glycol 6000 as precipitant. The crystals belong to space group C2, with unit-cell parameters a = 98.1, b = 74.3, c = 92.2 A, beta = 105.9 degrees. A native data set with a resolution of 2.44 A resolution has been collected. The approximate orientation of the haem group with respect to the unit-cell axes has been determined from the optical properties of the crystals.

PMID: 11679760 [PubMed - indexed for MEDLINE]

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