Supporting Online Material


Atomic Structure of Human Adenovirus by Cryo-EM Reveals Interactions Among Protein Networks
Hongrong Liu, Lei Jin, Sok Boon S. Koh, Ivo Atanasov, Stan Schein, Lily Wu,
Z. Hong Zhou

Supporting Online Material

Materials and Methods
SOM Text
Figs. S1 to S10
Tables S1 to S5
References

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Other Supporting Online Material for this manuscript includes the following:

Movie S1 Radially colored surface view of the Ad5 reconstruction.
Movie S2 A triangular facet of the reconstructed density map of the icosahedral Ad5 capsid, starting with the outer surface � showing four types of hexon in different colors, protein IX magenta), penton base (straw) and penton fiber (gray) � and rotating around to the inner surface � showing proteins IIIa (red), VI (yellow) and VIII (blue).
Movie S3 Example of an a helix from a hexon. The atomic model (stick) is superimposed on its cryoEM density map (mesh), starting in the same orientation as in Figure 1C. Note that all of the side chains are resolved.
Movie S4 Example of β strands from a hexon. The atomic model (stick) is superimposed on its cryoEM density map (mesh), starting in the same orientation as in Figure S2B. Note that the β strands are separated from one another and that the side chains are perpendicular to the plane of the β sheet.
Movie S5 Superposition of the atomic model (ribbon) of a hexon monomer on its semitransparent, gray, cryoEM density map, starting in the same orientation as in Figure S2A.
Movie S6 Protein IIIa. The backbone of its atomic model is superimposed on its semitransparent, gray, cryoEM density map, starting in the same orientation as in Figure 2B.
Movie S7 Protein VIII. The backbone of its atomic model is superimposed on its semitransparent, gray, cryoEM density map, starting in the same orientation as in Figure 2C.
Movie S8 The N-terminal trimer of protein IX, showing the N-joint. The backbones of the atomic models of the three contributing monomers (blue, red, and green sticks) are superimposed on their semi-transparent, gray, cryoEM density maps, starting in the same orientation as in Figure S5C.
Movie S9 The C-terminal four-helix bundle of protein IX. The backbone of the atomic models of the four contributing monomers (yellow, blue, and green sticks in one direction; red stick in the anti-parallel direction) are superimposed on their semi-transparent, gray, cryoEM density maps, starting in the same orientation as in Figure S5D.
Movie S10 Visualization of the rope domains of all four proteins IX by decreasing the density threshold of surface rendering. This density map was reconstructed with a B = 0Å2 to emphasize low-resolution features such as those (like the protein IX rope domain) with resolution degraded by modest flexibility, starting in the same orientation as in Figure S5E,F.