The pace of technological change in the field of macromolecular crystallography is quite breathtaking. The pursuits of particle physics have led to particle accelerators tailored for the production of synchrotron X-radiation of incredible intensity, geometric quality and wide tunable range.

The exploitation of this radiation, particularly the brilliance and use of short λ's, has made virus crystal data collection routine from difficult samples; although it is at present necessary to use hundreds of crystals in the gathering of just one data set. Maybe the use of ultra-short wavelength beams (≈0.33 Å) from a harmonic of an undulator could be harnessed to improve the lifetime of one such sample sufficiently to give a complete data set. Much larger macromolecular assemblies are currently under study, such as the ribosome, which possess little or no symmetry (unlike viruses) and are therefore more difficult to solve.

The revival of the Laue technique has been made possible by the polychromatic nature of the emitted spectrum and the associated high brightness. The study of time resolved phenomena in biological structures (as well as chemistry and solid state physics) with this method is a major research and development effort that is under way.

The interpretation of the diffuse scattering from macromolecular crystals will provide increasing information on the mobility of macromolecules.