Dysferlin is a large protein with numerous identified functional domains. The identified domains include seven C2 domains, a central DysF domain, and others common to the ferlin protein family. The three dimensional folding structure of each domains is unknown, as is whether the whole protein has a defined folding topology. This project will determine the folding structure of dysferlin’s functional domains by X-ray crystallography using crystallization of isolated and purified recombinant dysferlin domains. The folding structure of each domain will help define the function and potential interactions of dysferlin, and map specific missense mutations onto characterized structural domains providing a better understanding of their pathogenicity.