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Structure paper

TitleSelf-assembled superstructure alleviates air-water interface effect in cryo-EM.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 7300, Year 2024
Publish dateAug 24, 2024
AuthorsLiming Zheng / Jie Xu / Weihua Wang / Xiaoyin Gao / Chao Zhao / Weijun Guo / Luzhao Sun / Hang Cheng / Fanhao Meng / Buhang Chen / Weiyu Sun / Xia Jia / Xiong Zhou / Kai Wu / Zhongfan Liu / Feng Ding / Nan Liu / Hong-Wei Wang / Hailin Peng /
PubMed AbstractCryo-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- ...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.
External linksNat Commun / PubMed:39181869 / PubMed Central
MethodsEM (single particle)
Resolution2.56 - 3.9 Å
Structure data

34974

8hri

EMDB-34974, PDB-8hri:
SARS-CoV-2 Delta variant spike protein
Method: EM (single particle) / Resolution: 2.9 Å

34975

8hrj

EMDB-34975, PDB-8hrj:
SARS-CoV-2 Delta variant spike protein
Method: EM (single particle) / Resolution: 3.1 Å

34976

8hrk

EMDB-34976, PDB-8hrk:
SARS-CoV-2 Delta S-RBD-ACE2 complex
Method: EM (single particle) / Resolution: 3.3 Å

34977

8hrl

EMDB-34977, PDB-8hrl:
SARS-CoV-2 Delta S-RBD-ACE2
Method: EM (single particle) / Resolution: 2.8 Å

34978

8hrm

EMDB-34978, PDB-8hrm:
Cryo-EM structure of streptavidin
Method: EM (single particle) / Resolution: 2.56 Å

34979

8hrn

EMDB-34979, PDB-8hrn:
Cryo-EM structure of ACE2
Method: EM (single particle) / Resolution: 3.9 Å

34980

8hru

EMDB-34980, PDB-8hru:
Cryo-EM structure of ACE2
Method: EM (single particle) / Resolution: 3.9 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
  • streptomyces avidinii (bacteria)
KeywordsVIRAL PROTEIN / SARS-CoV-2 / Delta / Spike protein / PROTEIN BINDING / ACE2 / RBD / CYTOSOLIC PROTEIN / Complex / receptor of SARS-CoV-2

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