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. Author manuscript; available in PMC: 2013 May 26.
Published in final edited form as: J Struct Biol. 2010 Jul 3;172(3):363–371. doi: 10.1016/j.jsb.2010.06.022

Fig. 6.

Fig. 6

Further comparisons of CP dimers in PsV-F, PsV-S, and raPBV. (A) Side views of the backbone trace of the CP dimer of each virus (CPA, blue; CPB, red), which occupies the asymmetric unit of the T=1 icosahedron. (B) Same as in panel A, but rotated by 90° (horizontal axis) to place the protruding domains closest to the viewer. Each dimer is also rotated by 37° counterclockwise on the page to match the angular orientation of the left front dimer in panel C. (C) Outside view of the capsid of each virus, constructed from only the Cα atoms of the CP shell domains (see Materials and methods). The two front CP dimers in each capsid are shown in cyan and pink instead of blue and red. The respective front dimers are labeled A–B and a–b.