Abstract
Structural biology methods using cryoEM and cryo-electron tomography (cryoET) have become major tools for studying macromolecular complexes that are intrinsically flexible and dynamic, and often function in higher-order assemblies that are difficult to purify. The study of these complexes and assemblies in situ using cryoET and subtomogram averaging at sub-nanometer to near-atomic resolutions, coupled with cryoFIB and correlative and integrative imaging, opens a new frontier in structural cell biology, as exemplified in virus infection in human cells.
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