The technique of X-ray crystallography will be used to study the three dimensional structure of hemocyanin, the oxygen transport protein found in arthropods and molluscs. The invertebrate hemocyanins are particularly interesting because the oxygen binding site consists of two copper ions ligated directly by protein side chains. The exact nature and geometry of these metal sites are still in question. The major goal of the proposed research is to obtain diffraction data, determine and refine the oxygenated structure of a subunit of hemocyanin in order to understand how the oxygen molecule binds to the binuclear cooper site.
