Crystallization of quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni: crystals with unique optical properties.
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.
Oubrie
A
A
Laboratory of Biophysical Chemistry and BIOSON Research Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Huizinga
E G
EG
Rozeboom
H J
HJ
Kalk
K H
KH
de Jong
G A
GA
Duine
J A
JA
Dijkstra
B W
BW
D000429:Alcohol Oxidoreductases / Q000737:chemistry*; D020604:Comamonas testosteroni / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation
D000429:Alcohol Oxidoreductases; C019641:alcohol dehydrogenase (acceptor)