Time resolved X-ray diffraction experiments in single muscle fibres of the frog at 2.15 microns sarcomere length and 4 degrees C were performed at ID2 (SAXS), ESRF, Grenoble (France) to investigate the structural aspects of cross-bridge action during the development of the isometric tetanic tension (T0). Changes in the low angle myosin-based reflections were measured with 5 ms time resolution by signal averaging data collected with a 10 m camera length and a 2D gas-filled detector. Upon activation the intensity of the first order myosin layer line reflection, I(M1), and the intensity of the second order meridional reflection, I(M2), reduced practically to zero with a half-time which leads the tension rise by 15-20 ms. The complex changes of the intensity of the third order myosin meridional reflection, I(M3), and the increase of its axial spacing from 14.34 nm (at rest) to 14.57 nm (at T0) could be analysed by assuming that they were the result of the combination of the time dependent modulation in intensity of two closely spaced periodicities, one at 14.34 nm, characteristics of the myosin molecule at rest and the other at 14.57 nm, assumed by the myosin as a consequence of the activation and force production. I(14.34) drops monotonically in advance to isometric tension development with a half-time similar to that of I(M1) and I(M2), while I(14.57) rises from zero to a maximum in parallel with tension.