Fig. 2
From: Structural basis for the homotypic fusion of chlamydial inclusions by the SNARE-like protein IncA
Analysis of the conformational flexibility of IncA87–246 reveals two features. a Graphic representation of IncA87–246 anisotropically refined B-factor plotted onto the 3D-structure: the diameter of the tube is proportional to the B-factor. The hinge region and the moiety C-terminal of the Hclamp (in cyan) deviate by more than two standard deviations from the mean B-factor. b Crystal structure of IncA87–246(G144A) (protomer A), refined at 1.95 Å resolution (Table 1) with α-helices and random coiled linkers colored in red and green, respectively. c Secondary structure superimposition of IncA87–246(G144A) (green and red) with IncA87–246 (red and cyan). d Magnified view of IncA87–246 viewed down the main helical axis. Residues mutated to Ala in IncA87–246(polyA) are shown as sticks
