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8JWH

Cryo-EM structure of apo-state huamn angiotensin-converting enzyme 2 (ACE2)

Summary for 8JWH
Entry DOI10.2210/pdb8jwh/pdb
EMDB information36683
DescriptorProcessed angiotensin-converting enzyme 2 (1 entity in total)
Functional Keywordsreceptor, sars-cov-2, viral infection, hydrolase
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight69153.66
Authors
Yang, Z.,Wang, H.W. (deposition date: 2023-06-29, release date: 2024-07-03, Last modification date: 2025-01-22)
Primary citationYang, Z.,Fan, J.,Wang, J.,Fan, X.,Ouyang, Z.,Wang, H.W.,Zhou, X.
Electrospray-assisted cryo-EM sample preparation to mitigate interfacial effects.
Nat.Methods, 21:1023-1032, 2024
Cited by
PubMed Abstract: Addressing interfacial effects during specimen preparation in cryogenic electron microscopy remains challenging. Here we introduce ESI-cryoPrep, a specimen preparation method based on electrospray ionization in native mass spectrometry, designed to alleviate issues associated with protein denaturation or preferred orientation induced by macromolecule adsorption at interfaces. Through fine-tuning spraying parameters, we optimized protein integrity preservation and achieved the desired ice thickness for analyzing target macromolecules. With ESI-cryoPrep, we prepared high-quality cryo-specimens of five proteins and obtained three-dimensional reconstructions at near-atomic resolution. Our findings demonstrate that ESI-cryoPrep effectively confines macromolecules within the middle of the thin layer of amorphous ice, facilitating the preparation of blotting-free vitreous samples. The protective mechanism, characterized by the uneven distribution of charged biomolecules of varying sizes within charged droplets, prevents the adsorption of target biomolecules at air-water or graphene-water interfaces, thereby avoiding structural damage to the protein particles or the introduction of dominant orientation issues.
PubMed: 38664529
DOI: 10.1038/s41592-024-02247-0
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.34 Å)
Structure validation

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