5W5F
Cryo-EM structure of the T4 tail tube
Summary for 5W5F
Entry DOI | 10.2210/pdb5w5f/pdb |
EMDB information | 8767 |
Descriptor | Tail tube protein gp19 (1 entity in total) |
Functional Keywords | t4 tail tube, dose limit, helical reconstruction, viral protein |
Biological source | Enterobacteria phage T4 sensu lato |
Total number of polymer chains | 18 |
Total formula weight | 332633.03 |
Authors | Zheng, W.,Wang, F.,Taylor, N.M.,Guerrero-Ferreira, R.C.,Leiman, P.G.,Egelman, E.H. (deposition date: 2017-06-15, release date: 2017-08-16, Last modification date: 2024-03-13) |
Primary citation | Zheng, W.,Wang, F.,Taylor, N.M.I.,Guerrero-Ferreira, R.C.,Leiman, P.G.,Egelman, E.H. Refined Cryo-EM Structure of the T4 Tail Tube: Exploring the Lowest Dose Limit. Structure, 25:1436-1441.e2, 2017 Cited by PubMed Abstract: The bacteriophage T4 contractile tail (containing a tube and sheath) was the first biological assembly reconstructed in three dimensions by electron microscopy at a resolution of ∼35 Å in 1968. A single-particle reconstruction of the T4 baseplate was able to generate a 4.1 Å resolution map for the first two rings of the tube using the overall baseplate for alignment. We have now reconstructed the T4 tail tube at a resolution of 3.4 Å, more than a 1,000-fold increase in information content for the tube from 1968. We have used legacy software (Spider) to show that we can do better than the typical 2/3 Nyquist frequency. A reasonable map can be generated with only 1.5 electrons/Å using the higher dose images for alignment, but increasing the dose results in a better map, consistent with other reports that electron dose does not represent the main limitation on resolution in cryo-electron microscopy. PubMed: 28757144DOI: 10.1016/j.str.2017.06.017 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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