Oppositely charged globular protein and surfactant systems, such as lysozyme-sodium dodecyl sulfate (SDS) and ovalbumindodecyltrimethylammonium chloride (DOTAC) form precipitate, gel, and colorless solution in water over a wide concentration range. Bluish solutions are also recognized in connection with the redissolution of precipitate as well as prior to the gel formation. For the lysozyme-SDS system the bluish solution has been suggested to consist of finely dispersed gel particles in solution. The oppositely charged bovine serum albumin (BSA)-DOTAC-water system forms only a large, clear solution phase and a narrow, bluish solution region within a very limited surfactant concentration range. In the lysozyme-SDS system the formation of protein-surfactant aggregates and their growth and breakdown are studied in detail by cryogenic-transmission electron microscopy (cryo-TEM) method. In particular a series of samples with an increased surfactant concentration at fixed 4 wt% of lysozyme is studied. Imaging of the bluish solution at different protein concentrations exhibits large aggregates in the form of rod-like, sheet-like, and star-like objects which are attributed to the gel. At excess amounts of SDS, in the colorless solution, only small objects are detected. In the ovalbumin-DOTAC-water and BSA-DOTAC-water systems large aggregates are also observed in the bluish solutions. Colorless solutions for these two systems show the presence of small objects in the cryo-TEM micrographs. Ultrathin sections of the lysozyme and ovalbumin gels fixed with OsO 4 also show the presence of aggregated structures as judged from the transmission electron microscopy observations.