O. Elkabbani et al., CRYSTALLIZATION AND PRELIMINARY STRUCTURE DETERMINATION OF PORCINE ALDEHYDE REDUCTASE FROM 2 CRYSTAL FORMS, Acta crystallographica. Section D, Biological crystallography, 49, 1993, pp. 490-496
Aldehyde reductase from porcine kidney has been crystallized from buff
ered ammonium sulfate solutions. Two crystal forms are monoclinic spac
e group P2(1), with a = 56.2, b = 98.1, c = 73.2 angstrom, beta = 112.
5-degrees and a = 92.4, b = 62. 1, c = 59.0 angstrom, beta = 94.60. A
third crystal form is hexagonal with a = b = 166.0, c = 66.0 angstrom,
alpha = beta = 90.0-degrees and gamma = 120.0-degrees. Molecular-repl
acement structure solutions have been successfully obtained for the tw
o monoclinic crystal forms. The crystallographic R factor at 8-2.8 ang
strom resolution for the two monoclinic crystal forms is currently 0.2
3 and 0.25, respectively. There are two molecules per asymmetric unit
related by a non-crystallographic twofold axis. The aldehyde reductase
models are supported by the arrangement of the molecules in their res
pective unit cells and by electron densities corresponding to amino-ac
id side chains not included in the search structures.