Using technologies like electron microscopy (EM) it is possible to capture molecular mechanisms in great detail, but not when these mechanisms are currently moving. The field of cryomicroscopy circumvents this limitation by freezing said mechanism in place using cryogenic fluids. Although initially X-ray crystallography was commonly used, the much more versatile EM is now the standard approach in the form of cryo-EM, with recent advances giving us unprecedented looks at the mechanisms that quite literally make our bodies move.
Myosin-5 working stroke and walking on F-actin. (Credit: Klebl et al., 2024)
The past years has seen many refinements in cryo-EM, with previously quite manual approaches shifting to microfluidics to increase the time resolution at which a molecular process could be frozen, enabling researchers to for example see the myosin motor proteins go through their motions one step at a time. Research articles on this were published previously, such as by [Ahmet Mentes] and colleagues in 2018 on myosin force sensing to adjust to dynamic loads. More recently, [David P. Klebl] and colleagues published a research article this year on the myosin-5 powerstroke through ATP hydrolysis, using a modified (slower) version of myosin-5. Even so, the freezing has to be done with millisecond accuracy to capture the myosin in the act of priming (pre-powerstroke).
The most amazing thing about cryo-EM is that it allows us to examine ..
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