We have engineered am etal-binding site into the novel artificial b-propeller protein Pizza. This new Pizza variant carries two nearly identical domains per polypeptide chain, and forms at rimer with three-fold symmetry.T he designed single metal ion binding site lies on the symmetry axis, bonding the trimer together.T wo copies of the trimer associate in the presence of cadmium chloride in solution, and very highresolution X-raycrystallographic analysis reveals ananocrystal of cadmium chloride,s andwiched between two trimers of the protein. This nanocrystal, containing seven cadmium ions lying in ap lane and twelve interspersed chloride ions,i st he smallest reported to date.Our results indicate the feasibility of using rationally designed symmetrical proteins to biomineralizen anocrystals with useful properties.