S. Ramaswamy et al., CRYSTALLIZATION AND CRYSTALLOGRAPHIC INVESTIGATIONS OF COD ALCOHOL-DEHYDROGENASE CLASS-I AND CLASS-III ENZYMES, FEBS letters, 350(1), 1994, pp. 122-124
Cod liver alcohol dehydrogenase of class-hybrid properties has been cr
ystallized as an NAD(+)-pyrazole complex in the monoclinic space group
P2(l) with cell dimensions a = 103.3 Angstrom, b = 47.4 Angstrom, c =
80.7 Angstrom,beta = 104.6 degrees, and with one dimer in the asymmet
ric unit. The position of the dimer molecule in the crystal was determ
ined by molecular replacement methods at 3.0 A resolution. The success
ful search model was the poly-alanine structure of the horse enzyme. S
ide chains were then replaced according to the amino acid sequence of
the cod enzyme, and the structure has been refined at 2.8 A to an R-fa
ctor of 0.26. Cod liver class III alcohol dehydrogenase crystallizes i
n the monoclinic space group C2 with cell dimensions a = 127.5 Angstro
m, b = 76.6 Angstrom, c = 93.4 Angstrom, P = 99.4 degrees and with pro
bably one dimer in the asymmetric unit.