The viscosity-temperature behavior of N4 virus solution was investigated by using a Zimm type viscometer. The role of ionic strength (LiBr) and pH in the viscositytemperature behavior was determined. Supporting measurements of the sedimentation coefficient, infectivity, and optical density are presented. The viscosity-temperature behavior generally includes a region of low viscosity, characteristic of the intact virus, followed, upon increasing temperature, by a rather abrupt increase of viscosity which corresponds to the ejection of native DNA from the protein shell, presumably through a suitable opening in the capside. The viscosity remains constant upon further increase of temperature until a second abrupt increase is observed which is shown to correspond to the degradation of the empty protein shell (ghost). Finally, at a still higher temperature, denaturation of DNA occurs. This sequence of events can be altered by changes in pH and ionic strength. Increasing LiBr concentration reduces the temperature of ghost degradation and raises the temperature of DNA ejection and DNA denaturation. It is suggested that polyelectrolyte effects play a controlling role in the ejection of native DNA and that the conformation of the latter within the protein shell is stabilized by a decrease of the electrostatic free energy due to the swamping effect of the co-ions.