Crustacyanin, the blue carapace pigment of the common lobster Homarus gammarus (L.), has been purified and crystallized. This chromoprotein has a minimum molecular weight of 36 000 based on the content of the carotenoid prosthetic group astaxanthin. The molecular weight in gel filtration measurements is about 650 000, corresponding to some 18 molecules of astaxanthin per molecule of protein. Crustacyanin, on dialysis against water, dissociates into particles of about 35 000 molecular weight, each apparently bearing one molecule of carotenoid. The dissociation is accompanied by a shift in the principal maximum of the absorption spectrum from 633 to 595 nm and is reversed upon addition of salt. Reversible dissociation also occurs in the presence of 3 M urea, 1 M potassium thiocyanate, 10% (v/v) dioxan or 10% (v/v) acetone. When the carotenoid is removed from crustacyanin with acetone, the resultant apoprotein has a mean molecular weight of about 20 000. It may be resolved by starch gel electrophoresis into several components of which two predominate. Crustacyanin, indistinguishable from the native material, can be reconstituted from apoprotein and carotenoid. Evidence from the behaviour of crustacyanin and its apoprotein at surfaces indicates that the tertiary and quaternary structures of the native protein are stabilized by the carotenoid. It is suggested that the quarternary structure of crustacyanin is induced by an interaction of the carotenoid molecules of the subunits, which in turn causes a change in configuration of the protein favourable to aggregation. The result is a micelle-like structure with a hydrophobic carotenoid core.