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. 2011 Nov 17;7(11):e1002388. doi: 10.1371/journal.ppat.1002388

Figure 3. Three-dimensional structures of Cp183 Capsid and Cp183 Capsid/SRPKΔ.

Figure 3

Cp183 capsid (A, B, C) and capsid/SRPKΔ (D, E, F) are displayed as exterior views (A, D), gray scale central sections (B, E), and interior views (C, F). Surface-shaded representations were contoured to account for 100% of the expected protein volume for a Cp183 capsid. The closed red arrow identifies the external SRPKΔ density at twofold vertices; the open red arrow highlights that the interior density attributable to the CTDs. Binding of SRPKΔ correlates with remodeling the capsid interior (compare B, C with E, F) resulting in the loss of CTD density under twofold vertices. All views are along an icosahedral twofold axis. The scale bar represents 10 nm.