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. 2009 Jan 7;37(4):1211–1224. doi: 10.1093/nar/gkn1046

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© 2009 The Author(s)

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 6. — Functional characterization of clinically isolated or in vitro selected MepR mutants. (A) Histograms of MUG units obtained from β-galactosidase assays for various MepR mutations. Measurements were made in the presence (+) and absence (–) of tetracycline, the addition of which causes MepR production. (B) Structural mapping of MepR mutations. The side chains of the mutated residues are shown as red sticks and labelled. One subunit is colored pink and the other blue. The secondary structure elements of one subunit are labelled.