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Clathrin plays an intimate part in the creation of vesicles in cells. The team's results show the structure of the portion of the clathrin molecule that is responsible for assembly and suggest how similar coupling may work in other proteins. When clathrin molecules assemble to form a polyhedral lattice, the legs of nearby triskelions hook around each other. More traditional crystallography techniques could not be used because the structure of the clathrin molecule changes too easily when different heavy metals are added to the crystal lattice to determine phases. For MAD phasing, the researchers substituted only selenomethionine for all of the methionine in the protein and collected diffraction data at four different wavelengths near the selenium K edge.