Fig. 1: Cryo-EM reconstruction of Pseudomonas phage Pa193. | Communications Biology

Fig. 1: Cryo-EM reconstruction of Pseudomonas phage Pa193.

From: Cryo-EM analysis of Pseudomonas phage Pa193 structural components

Fig. 1

a Composite map of the Pa193 virion with an extended tail. b 3D-reconstructions of phage Pa193 determined in this study: the capsid solved using icosahedral (I4 symmetry) reconstruction; the neck and tail determined using localized reconstruction; the baseplate determined picking the tail tip distal from the capsid with C6 symmetry imposed. c Fourier Shell Correlation (FSC) curves for all reconstructions determined in this study. All reconstructions were masked. d Representative densities corresponding to each cryo-EM SPA technique above. Major capsid protein residues 231–250 (purple) fit in the I4 icosahedral reconstruction; portal protein residues 183–188; 209–217 (green) fit into the C12 localized reconstruction; sheath initiator protein residues 92–106 (light blue) fit in the C6 baseplate reconstruction.

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