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. Author manuscript; available in PMC: 2012 Aug 18.
Published in final edited form as: Cell. 2010 Apr 15;141(3):472–482. doi: 10.1016/j.cell.2010.03.041

Figure 2. Atomic Model of the Aquareovirus ISVP.

Figure 2

(A) Cryo-EM density (cyan mesh) of a VP5 monomer superimposed on its atomic model (yellow; only backbone shown).

(B) Stereo view of the box from (A). Cryo-EM densities (gray mesh) are superimposed on its atomic model (magenta).

(C) Cryo-EM density (cyan mesh) of VP3A superimposed on its atomic model (yellow; only backbone shown).

(D) Cryo-EM densities (gray mesh) of the four boxed regions in (C) showing representative side chains. Cryo-EM densities (gray mesh) are superimposed on its atomic model (magenta). Box 1 also shows density for a carboxyl oxygen atom (arrow). The different aromatic amino acids, Trp, Tyr and Phe, in boxes 2-4 are readily distinguished.

(E) Complete atomic model of the ISVP. In the right half, removal of the VP5 coat reveals core proteins. Ribbon models of the atomic structures of the six conformers from four structural proteins are shown in the periphery: two VP3 conformers (Figure S1), two VP6 conformers (Figure S2 and Movie S2) one VP1 (Figure S3 and Movie S2), and one VP5. These atomic models are color-coded according to amino acid sequence from blue (N terminus) through green and yellow to red (C-terminus). The black triangle demarcates a VP5 trimer. See also Figure S2 and Movie S2.