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. Author manuscript; available in PMC: 2014 Oct 8.
Published in final edited form as: Structure. 2013 Sep 19;21(10):1848–1858. doi: 10.1016/j.str.2013.08.012

Figure 2. Structure of activated and oligomeric SgrAI.

Figure 2

(A) Top and side views showing the organization of helical asymmetric units (DBDs) within the SgrAI oligomers. Eight distinct DBDs have been segmented out of the cryo-EM map and are each colored differently. (B) Helical reconstruction of oligomeric SgrAI at 8.6 Å resolution, segmented into 11 individual DBDs and labeled by helical asymmetric unit. Protein components of units 1,4,6,7,9 and 2,3,5,8, 10, 11 are shaded light and dark, respectively. (C) Segmentation and different views of an individual helical asymmetric unit. Each helical asymmetric unit contains two monomeric SgrAI protein subunits (colored light and dark orange), and two copies of pre-cleaved DNA (both colored blue). (D) Flexibly fit coordinates of SgrAI (Dunten et al., 2008) into the EM density of a segmented helical asymmetric unit. Arrows mark DNA disorder in the terminal regions. Scale bar is 150 Å. See also Figure S2-S3 and Movie S1.