Fig. 3: Identification and annotation of Pa193 phage capsid and decorating proteins.
From: Cryo-EM analysis of Pseudomonas phage Pa193 structural components
a Cryo-EM reconstruction of Pa193 capsid measured at 3.5 Å resolution and displayed at 3.5 σ. Major capsid protein assembles as pentons are colored (green) or hexons (blue), and decorating protein forms a trimer at every three-fold vertex (yellow). b Cryo-EM localized reconstruction of Pa193 capsid five-fold vertex at 2.9 Å resolution. The map is displayed at 4.5 σ and has the same protein color scheme as in panel (a). c Overlay of the Pa193 capsid protein gp26 conformers found in the penton (green), hexon (blue), and icosahedral 3-fold hexon (yellow) (penton:hexon, RMSD 5.5 Å; hexon:icosahedral 3-fold hexon, RMSD 0.001 Å). Ribbon diagrams of the capsid protein assembled in a penton or as part of a hexon are also shown. d Ribbon diagram of the decorating protein gp25 (residues 1–211) assembled as a trimer.
