After the Revolution: Where X-Ray Crystallography Stands in Context with Electron Cryo-Microscopy
DOI:
https://doi.org/10.18192/osurj.v5i1.8046Abstract
Despite the surge of cryo-electron microscopy (cryo-EM) as a leading method for structural determination in recent years after its “resolution revolution,” X-ray crystallography continues to play a key and crucial role in the field of structural biology. Although cryo-EM makes it possible to resolve non-crystallizable macromolecules, X-ray crystallography remains more effective in achieving atomic resolution and has the ability to define side chain and ligand orientations and interactions, making it useful in the mechanistic and enzymological study of proteins. This review highlights X-ray crystallography and emphasizes that X-ray crystallography and cryo-EM remain complementary methods in determining macromolecular structures instead of the former being fully replaced by the latter. In this context, together with other methods for structural analysis, X-ray crystallography is shown to adapt to the evolving structural biology landscape.
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