EMD-34977

Single-particle
2.8 Å
EMD-34977 Deposition: 15/12/2022
Map released: 20/12/2023
Last modified: 01/01/2025
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-34977

SARS-CoV-2 Delta S-RBD-ACE2

EMD-34977

Single-particle
2.8 Å
EMD-34977 Deposition: 15/12/2022
Map released: 20/12/2023
Last modified: 01/01/2025
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Homo sapiens, Severe acute respiratory syndrome coronavirus 2
Sample: SARS-CoV-2 Delta S-RBD-ACE2 complex
Fitted models: 8hrl (Avg. Q-score: 0.472)

Deposition Authors: Xu J, Meng F, Liu N , Wang HW
Self-assembled superstructure alleviates air-water interface effect in cryo-EM.
Zheng L , Xu J, Wang W, Gao X, Zhao C , Guo W, Sun L , Cheng H , Meng F, Chen B, Sun W, Jia X, Zhou X , Wu K , Liu Z , Ding F , Liu N , Wang HW , Peng H
(2024) Nat Commun , 15 , 7300 - 7300
PUBMED: 39181869
DOI: doi:10.1038/s41467-024-51696-w
ISSN: 2041-1723
Abstract:
Cryo-electron microscopy (cryo-EM) has been widely used to reveal the structures of proteins at atomic resolution. One key challenge is that almost all proteins are predominantly adsorbed to the air-water interface during standard cryo-EM specimen preparation. The interaction of proteins with air-water interface will significantly impede the success of reconstruction and achievable resolution. Here, we highlight the critical role of impenetrable surfactant monolayers in passivating the air-water interface problems, and develop a robust effective method for high-resolution cryo-EM analysis, by using the superstructure GSAMs which comprises surfactant self-assembled monolayers (SAMs) and graphene membrane. The GSAMs works well in enriching the orientations and improving particle utilization ratio of multiple proteins, facilitating the 3.3-Å resolution reconstruction of a 100-kDa protein complex (ACE2-RBD), which shows strong preferential orientation using traditional specimen preparation protocol. Additionally, we demonstrate that GSAMs enables the successful determinations of small proteins (<100 kDa) at near-atomic resolution. This study expands the understanding of SAMs and provides a key to better control the interaction of protein with air-water interface.