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• W2509245132 abstract "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." @default.
• W2509245132 created "2016-09-16" @default.
• W2509245132 creator A5024200175 @default.
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• W2509245132 date "2016-09-07" @default.
• W2509245132 modified "2023-10-17" @default.
• W2509245132 title "How cryo-electron microscopy and X-ray crystallography complement each other" @default.
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• W2509245132 doi "https://doi.org/10.1002/pro.3022" @default.
• W2509245132 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5192981" @default.
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