The structure of Mengo virus was determined to 3.0 A resolution using human rhinovirus 14 as an initial phasing model at 8.0 A resolution. Oscillation diffraction photographs were collected at the Cornell High Energy Synchrotron Source using orthorhombic Mengo virus crystals. The crystal space group was P2(1)2(1)2(1), a = 441.4, b = 427.3 and c = 421.9 A, with one icosahedral particle per asymmetric unit, giving 60-fold noncrystallographic redundancy. The orientations of the four viral particles in the unit cell were determined with a rotation function. Their positions relative to the crystallographic symmetry axes were found by a combination of Patterson-function analysis and a subsequent R-factor search using human rhinovirus 14 atomic coordinates as a model. The initial phases to 8.0 A resolution were then computed by placing human rhinovirus 14 particles in the orientations and positions of Mengo virus particles. These phases were improved by ten cycles of real-space molecular replacement averaging. Phases between 8.0 and 3.0 A resolution were obtained by molecular replacement phase extension. One or two reciprocal-space lattice points were used for each extension followed by two cycles of averaging.