Cryo-electron microscopy (Cryo-EM) has been offering impressive insights into the structures of macromolecules in the field of structural biology as a result of recent advancements in hardware and software technologies. This breakthrough has greatly aided our understanding of the cellular mechanisms of proteins and has triggered the dawn of an unprecedented golden age in structural biology. However, the technique still has inherent limitations owing to the dynamic tendency and tangled interactions of biomolecules. Attempts to overcome these limitations have led to the emergence of cryo-electron tomography (Cryo-ET) as a powerful technique in the field of structural biology, allowing for the three-dimensional visualization of the native conformation of biological specimens. This promising electron microscopy method has revolutionized our grasp of complex structures and their dynamic interactions, thereby providing unprecedented insights into the organization and function of macromolecular complexes within their native cellular environments. In this paper, we review state-of-the-art cryo-ET workflows, provide examples of biological applications, and discuss the fundamental necessity of boosting the potential applications of cryo-ET.
INTRODUCTION TO CRYO-EM TECHNOLOGY
GENERAL CONCEPTS OF TEM TO VISUALIZE BIOLOGICAL MOLECULES
PREPARATIVE WAY OF IMAGE ACQUISITION TO OBTAIN ELECTRON TOMOGRAM
TECHNOLOGICAL DEVELOPMENTS OF DED ACHIEVABLE HIGH-RESOLUTION CRYO-ET
STRUCTURAL DETERMINATION OF MACROMOLECULES BY USING CRYO-ET
HIGH-RESOLUTION CRYO-ET APPLICABLE TO LIFE SCIENCES
ACKNOWLEDGEMENTS
CONFLICT OF INTEREST
AUTHOR CONTRIBUTIONS
REFERENCES