Abstract
In modern life science research, structural information on proteins is indispensable for understanding the mechanisms of their biological functions. Many protein structures have been determined by X-ray crystallography, which has been developed in conjunction with molecular biology experiments and synchrotron radiation development. Since the Nobel Prize in Chemistry in 2017, the rapid progress of cryo-EM hardware and analysis software has led to the use of cryo-EM single-particle analysis for structural analysis. In this article, we compare the features of protein crystallography and cryo-EM single-particle analysis and discuss the best method for protein crystallography.
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