The photoreceptor membrane of Drosophila melanogaster (wild type, vitamin Adeprived wild type, and the mutants ninaA P228 , ninaB P3 ' S, and ora" 4) was studied by freezefracture electron microscopy . The three mutations caused a decrease in the number of particles on the protoplasmic face of the rhabdomeric membrane . The ninaA P228 mutation affected only the peripheral photoreceptors (R1-6), while the ninaB P315 mutation affected both the peripheral (R1-6) and the central photoreceptors (R7) . The ora JK84 mutation, which essentially eliminates R1-6 rhabdomeres, was found to drastically deplete the membrane particles in the vestigial R1-6 rhabdomeres but not in the normal rhabdomeres of R7 photoreceptors, suggesting that the failure of the ora JK84 mutant to form normal R1-6 rhabdomeres may be due to a defect in a major R1-6 photoreceptor-specific protein in the mutant . In all cases in which both the rhabdomeric particle density and rhodopsin content were studied, the mutations or vitamin A deprivation was found to reduce both these quantities, supporting the idea that at least the majority of the rhabdomeric membrane particles are closely associated with rhodopsin. Vitamin A deprivation and the mutations also reduced the number of particles in the plasma membrane as in the rhabdomeric membrane, suggesting that both classes of membrane contain rhodopsin .Freeze-fracture studies of the photoreceptors have shown that there are numerous membrane particles on the fracture face of both the outer segment disk membrane of vertebrate photoreceptors (36, 37, and references cited therein) and the rhabdomeric microvillar membrane of invertebrate photoreceptors (3,5,8,9,14,22,26,32) . Several lines of evidence suggest that these membrane particles are correlated with the presence of rhodopsin. For example, vitamin A deprivation, which reduces the rhodopsin content, has been found to reduce the number of disk membrane particles in vertebrate photoreceptors (16) and rhabdomeric membrane particles in invertebrate photoreceptors (3,14,22) .In the case of Drosophila, it is also possible to reduce the rhodopsin content by means of single-gene mutations. Among the mutants of Drosophila melanogaster that we have isolated for the study of the photoreceptor process are those with drastically reduced rhodopsin content (22,29,30) . The studies that have been carried out on some of these mutants suggest that the mechanism of rhodopsin depletion in these mutants can be very different from that of vitamin A deprivation (22) .