Volume 30, No 12, Dec 2020

ISSN: 1001-0602 
EISSN: 1748-7838 2018 
impact factor 17.848* 
(Clarivate Analytics, 2019)

Volume 30 Issue 12, December 2020: 1136-1139   |  Open Access

LETTERS TO THE EDITOR

Resolving individual atoms of protein complex by cryo-electron microscopy

Kaiming Zhang^1,* , Grigore D. Pintilie¹ , Shanshan Li¹ , Michael F. Schmid² , Wah Chiu^1,2,*

¹Department of Bioengineering and James H. Clark Center, Stanford University, Stanford, CA 94305, USA a
²Division of CryoEM and Bioimaging, SSRL, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA
Correspondence: Kaiming Zhang(kmzhang@stanford.edu)Wah Chiu(wahc@stanford.edu)

Dear Editor,

Breakthroughs in single-particle cryo-electron microscopy (cryo-EM) technology have made near-atomic resolution structure determination possible. Cryo-EM has resolved over four thousand structures at near-atomic resolutions (2–4 Å).1 It is rapidly becoming the method of choice for structure determination of membrane proteins, large assemblies, and multi-protein complexes partly because it does not require a crystal and partly because it can accommodate specimens with heterogeneous composition and/or conformation.2 This powerful technique is now capable of resolving protein complexes to better than 2 Å resolution3 and has been used to solve 3.7 Å resolution structure of RNA as small as ~40 kilodaltons.4

https://doi.org/10.1038/s41422-020-00432-2

FULL TEXT | PDF

Browse 822