MUSCLE contraction is driven by a cyclical interaction between the globular head domain of myosin and the actin filaments(1-6). We used quick stretches of 5 nm per half sarcomere to synchronize the movements of myosin heads in active single muscle fibres(5,7,8). The intensity of the 14.5 nm X-ray reflection decreased during the stretch, showing that the instantaneous elasticity of muscle(1,5) involves distortion of myosin heads. Head movement continued at about 1,500 s(-1) after the stretch, accompanied by partial force recovery. This indicates a reversal of the force-generating ’working stroke’ in the myosin heads(5,8,9) that is smaller and faster than assumed previously(5,10,11). By 50 ms after the stretch, myosin heads have regained both their original conformation and the ability to execute a normal working stroke. This ’repriming’ process is slower than that following shortening(12) but much faster than the ATP turnover rate per myosin head.