Scanning tunneling microscopy (STM) has been used as a method of studying the relationships between the enzymes of muscle glycogenolysis. In skeletal muscles the activation of phosphorylase b is catalyzed by phosphorylase kinase. This interaction is believed to occur in vivo as part of a multienzyme complex. The molecular structures of phosphorylase b and phosphorylase kinase have been visualized by STM.1 Phosphorylase b can be seen in dimeric and tetrameric forms as well as linear and circular aggregates. Individual molecules of phosphorylase kinase image as planar, bilobate structures with a twofold axis of symmetry and a central depression. STM has also been used to visualize complexes between phosphorylase kinase and its substrate, phosphorylase b.