Abstract
Many proteins function in the crystalline state, making crystallography a tool that can address mechanism, as well as structure. By initiating biological turnover in the crystal, transient structural species form, which may be filmed by Laue diffraction or captured by freeze-trapping methods. Laue diffraction has now reached an unprecedented level of sophistication and has found a 'niche of excellence' in the study of cyclic, ultra-fast, light-triggered reactions. Trapping methods, on the other hand, are more generally applicable, but require care to avoid artifacts. New strategies have been developed and difficulties such as radiation damage have received particular attention. Complementary methods--mainly UV/visible single-crystal spectroscopy--have proven essential to design, interpret and validate kinetic crystallography experiments.
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