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Single‐particle cryo‐electron microscopy (EM) is currently gaining attention for the ability to calculate structures that reach sub‐5 Å resolutions; however, the technique is more than just an alternative approach to X‐ray crystallography. Molecular machines work via dynamic conformational changes, making structural flexibility the hallmark of function. While the dynamic regions in molecules are essential, they are also the most challenging to structurally characterize. Single‐particle EM has the distinct advantage of being able to directly visualize purified molecules without the formation of ordered arrays of molecules locked into identical conformations. Additionally, structures determined using single‐particle EM can span resolution ranges from very low‐ to atomic‐levels (>30–1.8 Å), sometimes even in the same structure. The ability to accommodate various resolutions gives single‐particle EM the unique capacity to …