 0\) The asymmetric reconstructions of the hetero-pentamer (Figure 0F) and the monomeric P0 are very low-resolution compared to the icosahedral reconstruction. This is probably the result of incorrect image processing. The icosahedrally-averaged pentamer has resolutions extending well beyond 0 Å. Just by lowering the number of asymmetric units by 0-fold, the drop in resolution of the asymmetric reconstructions is too large. By keeping the orientations the same as in the original icosahedrally refined structure (i.e. by doing focussed classifications on the symmetry-expanded particles without re-alignments), resolutions around 0 Å should still be achievable in the asymmetric reconstructions. A good control is to perform a reconstruction of the symmetry expanded (partial signal subtracted) images without any classification/realignment, which should give a map that is almost identical to the icosahedrally averaged reconstruction. The authors should fix this mistake in a revised version, as it would yield a much higher-resolution, and thus more interesting, view on the asymmetry in the hetero-pentamer. In addition, the authors should present detailed views of the improved density, including side-chains, for regions where the sequence between P0 and P00 differ, which would then replace the ambiguous tracing of both proteins in the icosahedrally averaged map at two different thresholds in the current manuscript.  To some extent, the same argument also holds for the P0 monomer reconstruction: doing purely focussed classifications (without re-alignments) of symmetry-expanded images should also improve this part of the map. The only caveat (and cause for lower resolution) in this case would be different orientations of the P0 monomer relative to the capsid. However, even this may be captured better by focussed classifications without alignment than by the currently used focussed refinements.  0\) The paper would benefit greatly from extensive editing of the text, while carefully checking for grammar and spelling. In addition, the manuscript organization needs to be improved:  0.0) Previous knowledge hinting at the possible penton heteropentamer/double spike composition and organization is cited, but a clear account of the subject should appear in the Introduction. For instance: \"many models have been proposed\"... why? The authors should explain that the basis for these previous models is the sequence similarity between proteins P00 and P0 (see for example, Merckel et al., 0000; Huiskonen et al., 0000; Abrescia et al., 0000).  0.0) Also lacking is the information on how similar PRD0 and PR000 are at the genome level (Introduction, second paragraph, repeated in the third paragraph: \"a close relative\", how close? Should we expect large differences?).  0.0) The two alternative conformations of the P0 N-terminal tail are described twice: first in the third paragraph of the subsection "Penton base is a heteropentamer of P0 and P00", then in the fourth paragraph of the subsection "Overall Architecture of PR000".  0.0) The description of the different conformations of the P0 termini in the subsection "Major Capsid Protein and its conformations" is difficult to follow. For example, \"the helix... is not embedded deeply into the adjacent subunit of the trimer...\": what is meant here? And \"the loop formed by Tyr000-Val000 is flipped...\": flipped how? Perhaps a superposition of the twelve P0 monomers in the asymmetric units, zooming on the N- and C-termini, would help to better illustrate the mobility of these regions. In general, adding labels to the figures would help the reader to follow the structure description. For example, for some of the residues cited in the text; or for at least one occurrence of each of the P0 N- and C-terminal conformations in Figure 0.  0.0) Including the length of proteins and of their traced part in the Results section would also help the reader (without having to resort to the PDB validation report)