Abstract
Modern macromolecular crystallography has the potential, together with NMR, to provide an accurate description of structural changes produced by pressure in a macromolecular system. In particular, promoting and trapping higher-energy conformations of biological significance is of particular interest to explore functional mechanisms. An overview of this technique is given, including instrumentation and selected applications. This method is now fully-fledged and would deserve more interest from the structural biology community.