Open AccessSingle particle cryo-EM reconstruction of 52 kDa streptavidin at 3.2 Angstrom resolution
Author(s) -
Xinye Fan,
Jia Wang,
Xing Zhang,
Zi Yang,
Jincan Zhang,
Lingyun Zhao,
Hailin Peng,
Jianlin Lei,
Hongwei Wang
Publication year - 2019
Publication title -
nature communications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.559
H-Index - 365
ISSN - 2041-1723
DOI - 10.1038/s41467-019-10368-w
Subject(s) - streptavidin , cryo electron microscopy , resolution (logic) , single particle analysis , particle (ecology) , angstrom , macromolecule , molecule , materials science , graphene , nanotechnology , biophysics , electron microscope , chemistry , crystallography , chemical physics , biotin , physics , optics , biology , biochemistry , computer science , ecology , aerosol , organic chemistry , artificial intelligence
The fast development of single-particle cryogenic electron microscopy (cryo-EM) has made it more feasible to obtain the 3D structure of well-behaved macromolecules with a molecular weight higher than 300 kDa at ~3 Å resolution. However, it remains a challenge to obtain the high-resolution structures of molecules smaller than 200 kDa using single-particle cryo-EM. In this work, we apply the Cs-corrector-VPP-coupled cryo-EM to study the 52 kDa streptavidin (SA) protein supported on a thin layer of graphene and embedded in vitreous ice. We are able to solve both the apo-SA and biotin-bound SA structures at near-atomic resolution using single-particle cryo-EM. We demonstrate that the method has the potential to determine the structures of molecules as small as 39 kDa.