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. doi: 10.1107/s0907444901013002. Epub 2001 Oct 25.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcohol Oxidoreductases / chemistry*
  • Comamonas testosteroni / enzymology*
  • Crystallization
  • Crystallography, X-Ray
  • Protein Conformation


  • Alcohol Oxidoreductases
  • alcohol dehydrogenase (acceptor)