Chilling protein crystals enables the characterization of transient structural intermediatesConventional X-ray crystallography is useful for looking at macromolecular structures that are stable at ambient temperatures. But in enzymic and even in binding processes, intermediate structures are often more informative. By their nature, of course, intermediate structures do not last long enough under normal conditions to obtain X-ray diffraction data. However, by cooling protein samples to within a few tens of Kelvin of absolute zero, the lifetime of the intermediate states can be extended and their structures determined.
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