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. Author manuscript; available in PMC: 2016 Jan 31.
Published in final edited form as: Mol Microbiol. 2014 Dec 8;95(3):365–382. doi: 10.1111/mmi.12855

Figure 2. 1.25 Å crystal Structure of CT009 from C. trachomatis adopts an “open” fold, resulting in a subdomain swap dimer.

Figure 2

A. Crystal structure of C. trachomatis CT009 (residues 1 to 103) shown in cartoon ribbon format (colored blue (N-terminus) to red (C-terminus)). A single copy of CT009 is found within the asymmetric unit. Crystal structure is rotated 90° about the horizontal axis on the right.

B. Crystallographic dimer of CT009 mediated by “open” fold is depicted in cartoon ribbon format (colored orange and cyan, respectively) and is generated by applying the following symmetry operator: [y,x,-z].

C. 2Fo-Fc electron density map (blue mesh, contoured at 3.0σ) of the CT009 “hinge” region where subdomain swap dimerization occurs (residues Ile53 – Ala58). Coloring is the same as panel B.