Published online by Cambridge University Press: 14 March 2018
A key to understanding the function of biological systems is the visualization of their natural state, ideally in a natural environment. At a molecular level, this is challenging. Traditional experimental techniques, like X-ray crystallography, can provide the atomic structure of proteins, but only by removing them from their native surroundings and forcing them into crystals. Over the past decade, microscopy techniques have emerged as alternatives to these traditional structure determination methods, with the advantage of visualizing molecules in a near-native state. Given the current focus of structural biology on interactions between proteins and better understanding of large protein complexes, cryo-electron microscopy (cryo-EM) has become a valuable tool.