摘要
A founding principle of structural biology is that,once researchers can directly observe macromolecules at sufficient resolution,it should be possible to understand how their 3D structures confer their biological functions.In two studies published concurrently in the October 2020 issue of the journal Nature,Yip et al.[1]and Nakane et al.[2]reported the sharpest images yet obtained by using single-particle cryo-EM,enabling the location of individual atoms in a protein to be determined for the first time.Both teams used improved hardware that broke the previous resolution limitations of cryo-EM imaging.With the development of these technologies,the increased signal-to-noise ratio of cryo-EM images will expand the technique’s applicability.Combining these technologies may make it possible to determine biological structures with cryo-EM at a resolution even beyond 1 A(0.1 nm)-an achievement that was near impossible in the past.
