Crystallization of quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni: crystals with unique optical properties.
Article Details
- CitationCopy to clipboard
Oubrie A, Huizinga EG, Rozeboom HJ, Kalk KH, de Jong GA, Duine JA, Dijkstra BW
Crystallization of quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni: crystals with unique optical properties.
Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1732-4. Epub 2001 Oct 25.
- PubMed ID
- 11679760 [ View in PubMed]
- Abstract
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.