  Microsecond time-resolved cryo-electron microscopy has emerged as a novel
approach for directly observing proteins dynamics. By providing microsecond
temporal and near-atomic spatial resolution, it has the potential to elucidate
a wide range of dynamics that were previously inaccessible and therefore, to
significantly advance our understanding of protein function. This review
summarizes the properties of the laser melting and revitrification process that
underlies the technique and describes different experimental implementations.
Strategies for initiating and probing dynamics are discussed. Finally, the
microsecond time-resolved observation of the capsid dynamics of CCMV, an
icosahedral plant virus, is reviewed, which illustrates important features of
the technique as well as its potential.
