Cryo-EM structures of both ends of the actin filament explain why the barbed end elongates faster than the pointed end.

Cells depend cytoplasmic filaments assembled from the protein actin for their physical integrity, as tracks for myosin motor proteins and movements of the whole cell and internal organelles. Actin filaments elongate and shrink at their ends by adding or dissociating single actin molecules. We used cryo-electron microscopy to determine the structures of the two ends of actin filaments at 3.5 Å resolution for the slowly growing pointed end and 3.1 Å for the rapidly growing barbed end. These structures reveal why barbed ends grow faster than the pointed ends, why the rate at the pointed end is not diffusion-limited and why the pointed end has a low affinity for the γ-phosphate released from bound ATP inside the filament.