Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aquifex aeolicus.

A protein disulfide oxidoreductase from the thermophilic bacterium Aquifex aeolicus has been overexpressed in Escherichia coli and crystallized at 298 K using the hanging-drop vapour-diffusion method. Crystals belong to space group R32, with unit-cell parameters a = b = 161.1, c = 153.1 Å. A complete data set has been collected to 2.4 Å using synchrotron radiation. Packing-density considerations agree with the presence of 2-4 monomers in the asymmetric unit, with a corresponding solvent content of 66-32%.