EMD-0689

Single-particle
3.2 Å
EMD-0689 Deposition: 15/01/2019
Map released: 29/05/2019
Last modified: 27/03/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-0689

The reconstruction of biotin-bound streptavidin at 3.2 Angstrom resolution

EMD-0689

Single-particle
3.2 Å
EMD-0689 Deposition: 15/01/2019
Map released: 29/05/2019
Last modified: 27/03/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Streptomyces avidinii
Sample: Streptavidin with biotin
Fitted models: 6j6j (Avg. Q-score: 0.517)
Raw data: EMPIAR-10270

Deposition Authors: Fan X , Wang J, Lei JL, Wang HW
Single particle cryo-EM reconstruction of 52 kDa streptavidin at 3.2 Angstrom resolution.
Fan X , Wang J, Zhang X, Yang Z, Zhang JC, Zhao L, Peng HL , Lei J , Wang HW
(2019) Nat Commun , 10 , 2386 - 2386
PUBMED: 31160591
DOI: doi:10.1038/s41467-019-10368-w
ISSN: 2041-1723
Abstract:
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.