5W5E

Re-refinement of the pyocin tube structure

Summary for 5W5E

• Entry DOI: 10.2210/pdb5w5e/pdb
• EMDB information: 6270
• Descriptor: FIIR2 protein (1 entity in total)
• Functional Keywords: pyocin, bacteriocin, structural protein
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 30
• Total formula weight: 542656.41

Authors

Wang, F.,Zheng, W.,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

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: 28757144
DOI: 10.1016/j.str.2017.06.017

Experimental method

ELECTRON MICROSCOPY (3.5 Å)