Abstract
Myosin filaments interact with actin to generate muscle contraction and many forms of cell motility. X-ray and electron microscopy (EM) studies have revealed the general organization of myosin molecules in relaxed filaments, but technical difficulties have prevented a detailed description. Recent studies using improved ultrastructural and image analysis techniques are overcoming these problems. Three-dimensional reconstructions using single-particle methods have provided many new insights into the organization of the myosin heads and tails. Docking of atomic structures into cryo-EM density maps suggests how regulated myosin filaments are 'switched off', bringing about muscle relaxation. Additionally, sequence analysis suggests probable interactions between myosin tails in the backbone, whereas crystallographic and EM studies are starting to reveal tail interactions directly in three dimensions.
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