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. Author manuscript; available in PMC: 2014 Nov 1.
Published in final edited form as: J Struct Biol. 2013 Oct 7;184(2):10.1016/j.jsb.2013.09.022. doi: 10.1016/j.jsb.2013.09.022

Fig. 8. Comparison of the relative secondary structure in EspBmtu, EspBmtu-N and EspBmtu-C.

Fig. 8

A. Disorder predictions for EspBmtu with location of the predicted PE and PPE domains indicated by rectangles.

B. CD spectra of EspBmtu (black long dashed line), EspBmtu-N (blue short dashed line) and EspBmtu-C (red solid line). Data are expressed as molar ellipticity. EspBmtu-N (residues 1–358) was produced recombinantly and EspBmtu-C was obtained as a mixture of two proteolytic fragments (residues 359–460 and 387–460) as described in Methods.