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. Author manuscript; available in PMC: 2015 Aug 1.
Published in final edited form as: J Struct Biol. 2014 Jul 3;187(2):95–102. doi: 10.1016/j.jsb.2014.06.008

Fig. 1. CryoEM of in vitro assembled baseplates.

Fig. 1

The five recombinant wedge proteins (gp10, 7, 8, 6, and 53) self-assemble into a hubless baseplate-like structure. The diameter of a particle is about 480 Å. (a) Top view and (b) side view. Note that in (b) many of the particles can be seen stacking on top of each other in a manner similar to their packing on the 6-fold crystallographic axis in the hexagonal crystals. (c) The molecular replacement search model constructed from the independently determined partial structures of trimeric gp10 (yellow), dimeric gp6 (beige) and the complete structure of dimeric gp8 (blue), positioned into a wedge (outlined in green) of the star-shaped baseplate (outlined in black) as determined from the cryoEM analysis of a T4 tail. The center of the baseplate is indicated by a cross.