Single-Particle Cryo-EM at Crystallographic Resolution
Until only a few years ago, single-particle electron cryo-microscopy (cryo-EM) was usually not the first choice for many structural biologists due to its limited resolution in the range of nanometer to subnanometer. Now, this method rivals X-ray crystallography in terms of resolution and can be used...
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Published in | Cell Vol. 161; no. 3; pp. 450 - 457 |
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Main Author | |
Format | Journal Article |
Language | English |
Published |
United States
23.04.2015
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Subjects | |
Online Access | Get full text |
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Summary: | Until only a few years ago, single-particle electron cryo-microscopy (cryo-EM) was usually not the first choice for many structural biologists due to its limited resolution in the range of nanometer to subnanometer. Now, this method rivals X-ray crystallography in terms of resolution and can be used to determine atomic structures of macromolecules that are either refractory to crystallization or difficult to crystallize in specific functional states. In this review, I discuss the recent breakthroughs in both hardware and software that transformed cryo-microscopy, enabling understanding of complex biomolecules and their functions at atomic level. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 ObjectType-Review-3 content type line 23 |
ISSN: | 0092-8674 1097-4172 1097-4172 |
DOI: | 10.1016/j.cell.2015.03.049 |