  We present a study on filamentous actin solutions containing heavy meromyosin
subfragments of myosin II motor molecules. We focus on the viscoelastic phase
behavior and internal dynamics of such networks during ATP depletion. Upon
simultaneously using micro-rheology and fluorescence microscopy as
complementary experimental tools, we find a sol-gel transition accompanied by a
sudden onset of directed filament motion. We interpret the sol-gel transition
in terms of myosin II enzymology, and suggest a "zipping" mechanism to explain
the filament motion in the vicinity of the sol-gel transition.
