The ultrastructure of Drosophila melanogaster cytoplasmic ribosomal subunits and monomers have been examined by electron microscopy. The Drosophila ribosomal structures are compared to those determined for other eucaryotes and E. coli. Negatively contrasted images of 60S subunits are seen in the most frequent view to be approximately round particles about 280 A in diameter. About 35% of the particles present a single prominent projection which we call the 60S peak. The peak emanates from a flattened region of the 60S subunit. The maximum observed length of the 60S peak is approximately 90 A. The Drosophila 60S peak is highly reminiscent of the E. coli L7/L12 stalk. The Drosophila 40S subunit is an elongated, slightly bent particle which measures 280 X 170 X 160 A. It bears a strong resemblance to small ribosomal subunits of other eucaryotes and is strikingly similar to the E. coli 30S subunit. Micrographs of 80S monomeric ribosomes show the long axis of the 40S to be parallel and in apparent contact with the flattened region of 60S subunit. The 60S peak appears to bisect the long axis of the 40S subunit. The 40S subunit seems to be oriented in the monomeric ribosome so that the 40S projection is toward the body of the large subunit. Comparison of our data with similar studies in different organisms indicates that the eucaryotic large ribosomal subunits exhibit morphological heterogeneity while the small subunits remain remarkably similar.