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Protein Sci. 2017 Jan;26(1):32-39. doi: 10.1002/pro.3022. Epub 2016 Sep 7.

How cryo-electron microscopy and X-ray crystallography complement each other.

Author information

1
Beijing Advanced Innovation Center for Structural Biology, Ministry of Education Key Laboratory of Protein Sciences School of Life Sciences, Tsinghua University, Beijing, 100084.
2
Tsinghua-Peking Joint Center for Life Sciences, Tsinghua University, Beijing, 100084.

Abstract

With the ability to resolve structures of macromolecules at atomic resolution, X-ray crystallography has been the most powerful tool in modern structural biology. At the same time, recent technical improvements have triggered a resolution revolution in the single particle cryo-EM method. While the two methods are different in many respects, from sample preparation to structure determination, they both have the power to solve macromolecular structures at atomic resolution. It is important to understand the unique advantages and caveats of the two methods in solving structures and to appreciate the complementary nature of the two methods in structural biology. In this review we provide some examples, and discuss how X-ray crystallography and cryo-EM can be combined in deciphering structures of macromolecules for our full understanding of their biological mechanisms.

KEYWORDS:

X-ray and electron scattering; X-ray crystallography; cryo-EM; protein structure determination; structural biology; structure determination methods

PMID:
27543495
PMCID:
PMC5192981
DOI:
10.1002/pro.3022
[Indexed for MEDLINE]
Free PMC Article

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