Abstract
Cryogenic electron microscopy (cryo-EM) and single-particle analysis now enables the determination of high-resolution structures of macromolecular assemblies that have resisted X-ray crystallography and other approaches. Successful high-resolution structure determination by cryo-EM always depends on the quality of the protein sample. While structural heterogeneity remains a key challenge for cryo-EM, it also represents a rare opportunity to study the intrinsic conformational flexibility of macromolecular assemblies. Here, we review the key technological advancements that have made this ‘resolution revolution’ possible and give a concise overview of the technical challenges that needed to be overcome to allow high-resolution structure determination.
Original language | English |
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Number of pages | 6 |
Journal | Current Opinion in Structural Biology |
Volume | 46 |
DOIs | |
Publication status | Published - 1 Oct 2017 |
Equipment
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Australian Synchrotron
Office of the Vice-Provost (Research and Research Infrastructure)Facility/equipment: Facility