Crystallization and preliminary structure determination of porcine aldehyde reductase from two crystal forms.
Aldehyde reductase from porcine kidney has been crystallized from buffered ammonium sulfate solutions. Two crystal forms are monoclinic, space group P2(1), with a = 56.2, b = 98.1, c = 73.2 A, beta = 112.5 degrees and a = 92.4, b = 62.1, c = 59.0 A, beta = 94.6 degrees. A third crystal form is hexagonal with a = b = 166.0, c = 66.0 A, alpha = beta = 90.0 degrees and gamma = 120.0 degrees. Molecular-replacement structure solutions have been successfully obtained for the two monoclinic crystal forms. The crystallographic R factor at 8-2.8 A resolution for the two monoclinic crystal forms is currently 0.23 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 respective unit cells and by electron densities corresponding to amino-acid side chains not included in the search structures.
The University of Alabama at Birmingham, Center for Macromolecular Crystallography, 35294-0005, USA.
O
O
El-Kabbani
L
L
Sthanam
V L
VL
Narayana
K M
KM
Moore
N C
NC
Green
T G
TG
Flynn
L J
LJ
Delucas