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Aldehyde reductase from porcine kidney has been crystallized from buffered ammonium sulfate solutions. Two crystal forms are monoclinic, space group P21, with a = 56.2, b = 98.1, c = 73.2 Å, β = 112.5° and a = 92.4, b = 62.1, c = 59.0 Å, β = 94.6°. A third crystal form is hexagonal with a = b = 166.0, c = 66.0 Å, α = β = 90.0° and γ = 120.0°. Molecular-replacement structure solutions have been successfully obtained for the two monoclinic crystal forms. The crystallographic R factor at 8–2.8 Å 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.
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