File:Fmicb-08-01241-g003.jpg

English: (A) Modeled 2D SDS-PAGE gel representing structural proteins of a type phage from each of the new Helgoland Pseudoalteromonas phage genera. Band width is based on mass spectroscopy-quantified peptide abundances, as calculated by the normalized spectral abundance factor (NSAF; 2006)—essentially the predicted relative abundance of each protein in the virion of each phage. The size of the “fragment” represented the per phage NSAF. The largest bands in each row (phage major capsid proteins) are shown with transparency to allow visualization of overlapping bands (all other black bands). Band vertical position is based on molecular weights predicted from amino acid sequences. (B) 3-D prediction of PSA-HS1 phage major capsid protein (HS1_00030) with cryo-EM resolved backbone (purple) of Bacillus subtilis bacteriophage SPP1 protein, gp13. (C) 3-D prediction of PSA-HS8 phage major capsid protein (HS8_00019) with cryo-EM resolved backbone (purple) of Bacillus subtilis bacteriophage SPP1 protein, gp13. (D) Reconstructed capsid of Bacillus subtilis bacteriophage SPP1 protein, comprised of multiple gp13 subunits, which are predicted to be analogous to the PSA-HS1- and PSA-HS2-like genera capsids.