Crystallization and preliminary X-ray diffraction studies of a novel alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix

A novel alcohol dehydrogenase enzyme has been cloned from the hyperthermophilic archaeon Aeropyrum pernix and overexpressed in Escherichia coli. This zinc‐containing enzyme has been crystallized by the sitting‐drop vapour‐diffusion method using PEG 600 as precipitant. The crystals diffract to 1.5 Å resolution and belong to the orthorhombic space group P21212, with unit‐cell parameters a = 100.7, b = 103.2, c = 67.5 Å. The asymmetric unit contains two enzyme monomers. Two synchrotron data sets have been collected: one at a wavelength near the absorption edge of zinc and one at a remote wavelength. Three strong zinc‐ion positions were visible in the anomalous Patterson map. Two additional weaker zinc ions have been identified by anomalous Fourier synthesis.