In the last ten years, single crystal X-ray diffraction studies have led to the elucidation of the tertiary structure of a number of globular proteins. These crystallographic studies have made possible the direct determination of three-dimensional structures in the solid state, the resolution of the actual configuration of enzymatic active sites, and they have stimulated attempts to formulate general principles of peptide chain folding. Since the early days of immunology, many models have been proposed to try to explain the properties of antibodies in terms of molecular configurations of the antigen-binding sites. As a result of physico-chemical studies of proteins associated with the immune response, a number of immunoglobulins and their fragments have been crystallized, opening the way for X-ray diffraction studies of these proteins. In this paper we will review our studies on the structure of the crystalline Fc fragment of normal rabbit and human myeloma IgG. Our results...