Abstract

Melittin is the principal protein component of bee venom and is believed to function as a lytic agent. In aqueous salt solution, it is a tetramer of identical peptides, each with 26 amino acid residues. Although its amino acid composition is unusually nonpolar, and although it is believed to integrate into membranes while lysing cells, melittin is water-soluble at neutral pH. Two crystal forms have been grown from solutions containing ammonium sulfate and sodium formate, and their x-ray diffraction patterns indicate that the melittin tetramer contains at least one 2-fold axis of rotation. Both crystal forms are suitable for high resolution x-ray structural studies. Moreover, both crystals bind several heavy atoms as judged by changes in buoyancy, so that phase determination by the method of isomorphous replacement is possible. Crystallized melittin retains its lytic activity even under the conditions of crystallization (about 70% saturated ammonium sulfate).