Abstract
Despite its established powerfulness, the attempt to apply protein crystallography to a certain specific object is often hampered by various technical barriers which exhaust the individuals and the institution involved in the project. The availability of X-ray beam produced by synchrotron (orbit) radiation (SOR or SR) is expected to widen the horizon of protein crystallography in at least three ways. (1) The speed-up of data collection due to intensity will enable us to tackle larger proteins of more biological significance and, to some extent, to study the time-dependent phenomenon occurring in single crystals. (2) The better quality of diffraction data due to intensity and smaller divergence will liberate us from the burden of making very large crystals and will enable us to use lighter heavy atoms in the isomorphous replacement method. (3) The intrinsic variability of wave length of SOR X-ray coupled with the better quality of data will make the use of anomalous scattering effect much more feasible for the solution of the phase problem.
