Screen‐less oscillation photography is the method of choice for recording three‐dimensional X‐ray diffraction data for crystals of biological macromolecules. The geometry of an oscillation camera is extremely simple. However, the manner in which the reciprocal lattice is recorded in any experiment is fairly complex. This depends on the Laue symmetry of the reciprocal lattice, the lattice type, the orientation of the crystal on the camera and to a lesser extent on the unit‐cell dimensions. Exploring the relative efficiency of collecting X‐ray diffraction data for different crystal orientations prior to data collection might reduce the number of films required to record most of the unique data and the consequent amount of time required for processing these films. Here algorithms are presented suitable for this purpose and results are reported for the 11 Laue groups, different lattice types and crystal orientations often employed in data c