Structural intermediates in a biological reaction may be monitored by
rapid spectroscopic or somewhat slower structural techniques. Intermed
iates may evolve in real time (no trapping), be stabilized by chemical
manipulation of the reactants, the macromolecule or the solvent (chem
ical trapping), or be stabilized by lowering the temperature (freeze t
rapping). The last is beginning to be coupled with X-ray diffraction,
electron cryomicroscopy and solid-state NMR approaches to characterize
the trapped intermediates. Care in conducting such experiments, toget
her with an awareness of possible artefacts, is essential if reliable
structural results are to be obtained.