Elucidation of the oligomerization mechanism of pore forming protein

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Pore forming proteins form oligomer on the surface of the cell. Then, they form an ion permiable pore to disrupt the cells. In this reseach, structural changes in oligomerization and oligomeric stucture of the pore forming proteins were measured by small-angle X-ray scattering (SAXS) and crystal X-ray diffraction. A hemolytic lectin from marine invertebrate Cucumaria echinata (CEL-III) forms heptamer at first then three heptamers form 21-mer and 21-mer dissociated to heptamer in the presence of detergent by the results of SAXS measurements. CEL-III oligomer was crystallized and X-ray diffraction data were collected. Crystals diffracted X-rays to 3.3 and 4.2 A resolution using synchrotron radiation.