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. 2011 Mar 4;30(8):1497–1507. doi: 10.1038/emboj.2011.58

Figure 3.

Figure 3

Fitting of atomic structures into the cryo-EM densities for the stalled ternary complexes. (A) Cryo-EM densities are shown for cognate and near-cognate A/T and EF-Tu in transparent magenta (tRNA) and grey/red (for cognate and near-cognate EF-Tu, respectively). The fitted structures are shown in ribbons. (B) Close-up view of superimposed fitted structures for cognate (coloured by domains) and near-cognate EF-Tu (in red). (C) Stereo-view representation of EF-Tu structures. Cognate EF-Tu fragments 1–202 (domain I), 203–300 (domain II) and 301–393 (domain III) are shown in cyan, green and yellow, respectively. Switch I, II and P loop of domain I are represented in darker blue. Fragments 219–226 and 256–273 of domain II are represented in darker green. The position of residues Val20, Ile60 and His84 is highlighted for comparison in both fitted structures. The EF-Tu complexes are aligned with respect to the 70S ribosomes. Supplementary Figure S3 depicts the stereo-view representation of the same EF-Tu complexes but aligned with respect to each other.