8HI2
Structure of EV71 VLP frozen at -183 degree embedded in crystalline ice
Summary for 8HI2
Entry DOI | 10.2210/pdb8hi2/pdb |
EMDB information | 32709 |
Descriptor | Genome polyprotein, Genome polyprotein (Fragment) (3 entities in total) |
Functional Keywords | virus |
Biological source | Enterovirus A71 More |
Total number of polymer chains | 3 |
Total formula weight | 77460.98 |
Authors | |
Primary citation | Shi, 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: 36586403DOI: 10.1016/j.str.2022.12.001 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
Download full validation report
