8JWH
Cryo-EM structure of apo-state huamn angiotensin-converting enzyme 2 (ACE2)
Summary for 8JWH
Entry DOI | 10.2210/pdb8jwh/pdb |
EMDB information | 36683 |
Descriptor | Processed angiotensin-converting enzyme 2 (1 entity in total) |
Functional Keywords | receptor, sars-cov-2, viral infection, hydrolase |
Biological source | Homo sapiens (human) |
Total number of polymer chains | 1 |
Total formula weight | 69153.66 |
Authors | Yang, Z.,Wang, H.W. (deposition date: 2023-06-29, release date: 2024-07-03, Last modification date: 2025-01-22) |
Primary citation | Yang, 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: 38664529DOI: 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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