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8HHS

Structure of human apoferritin embedded in crystalline ice

Summary for 8HHS
Entry DOI10.2210/pdb8hhs/pdb
EMDB information32703
DescriptorFerritin heavy chain (1 entity in total)
Functional Keywordsmetal binding protein
Biological sourceHomo sapiens (human)
Total number of polymer chains24
Total formula weight482797.13
Authors
Shi, H.,Wu, C.,Zhang, X. (deposition date: 2022-11-17, release date: 2023-02-15, Last modification date: 2024-07-03)
Primary citationShi, H.,Wu, C.,Zhang, X.
Addressing compressive deformation of proteins embedded in crystalline ice.
Structure, 31:213-220.e3, 2023
Cited by
PubMed Abstract: For cryoelectron microscopy (cryo-EM), high cooling rates have been required for preparation of protein samples to vitrify the surrounding water and avoid formation of damaging crystalline ice. Whether and how crystalline ice affects single-particle cryo-EM is still unclear. Here, single-particle cryo-EM was used to analyze three-dimensional structures of various proteins and viruses embedded in crystalline ice formed at various cooling rates. Low cooling rates led to shrinkage deformation and density distortions on samples having loose structures. Higher cooling rates reduced deformations. Deformation-free proteins in crystalline ice were obtained by modifying the freezing conditions, and reconstructions from these samples revealed a marked improvement over vitreous ice. This procedure also increased the efficiency of cryo-EM structure determinations and was essential for high-resolution reconstructions.
PubMed: 36586403
DOI: 10.1016/j.str.2022.12.001
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.4 Å)
Structure validation

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