Abstract
Abstract Ten years ago, the term “resolution revolution” was used for the first time to describe how cryogenic electron microscopy (cryo-EM) marked the beginning of a new era in the field of structural biology, enabling the investigation of previously unsolvable protein targets. The success of cryo-EM was recognized with the 2017 Chemistry Nobel Prize and has become a widely used method for the structural characterization of biological macromolecules, quickly catching up to x-ray crystallography. Bioenergetics is the division of biochemistry that studies the mechanisms of energy conversion in living organisms, strongly focused on the molecular machines (enzymes) that carry out these processes in cells. As bioenergetic enzymes can be arranged in complexes characterized by conformational heterogeneity/flexibility, they represent challenging targets for structural investigation by crystallography. Over the last decade, cryo-EM has therefore become a powerful tool to investigate the structure and function of bioenergetic complexes; here, we provide an overview of the main achievements enabled by the technique. We first summarize the features of cryo-EM and compare them to x-ray crystallography, and then, we present the exciting discoveries brought about by cryo-EM, particularly but not exclusively focusing on the oxidative phosphorylation system, which is a crucial energy-converting mechanism in humans.
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