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. Author manuscript; available in PMC: 2015 Nov 28.
Published in final edited form as: Nature. 2015 Mar 16;521(7553):545–549. doi: 10.1038/nature14247

Figure 4. Structure of the Φ-clamp.

Figure 4

a, Top view of the Φ-clamp region of the PA pore showing the cryoEM map (mesh) superimposed with the atomic model (stick). b, Tilted view of the Φ-clamp with seven protomers colored differently, showing the aromatic CH-π interaction. c, Cross-section side view of the translocation channel near the Φ-clamp region. The Φ-clamp (Phe427) and the conserved acidic residue Asp425 are colored in orange and red, respectively.