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The structure of auracyanin B, a `blue' copper protein produced by Chloroflexus aurantiacus, has previously been solved and refined in the hexagonal space group P6422 with a single molecule in the asymmetric unit. The protein has now been crystallized in space group P65, with unit-cell parameters a = b = 115.9, c = 108.2 Å. In the new crystal form, the asymmetric unit contains four protein molecules. The structure has been solved by molecular replacement and refined at 1.9 Å resolution. The final residuals are R  =  19.2% and Rfree  =  21.9%. In relation to the earlier crystal structure, the doubling of the unit-cell volume and the lower symmetry are explained by small rotations of the molecules with respect to one another.

Supporting information

PDB reference: auracyanin B, 1ov8, r1ov8sf


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