Directed movement is a characteristic of many living organisms and occ
urs as a result of the transformation of chemical energy into mechanic
al energy. Myosin is one of three families of molecular motors that ar
e responsible for cellular motility. The three-dimensional structure o
f the head portion of myosin, or subfragment-1, which contains both th
e actin and nucleotide binding sites, is described. This structure of
a molecular motor was determined by single crystal x-ray diffraction.
The data provide a structural framework for understanding the molecula
r basis of motility.