1. Same Same but Different: New Structural Insight into CRISPR-Cas Complexes 
Nadja Heidrich, Jörg Vogel 
Molecular Cell 
Volume 52, Issue 1, Pages 4-7 (October 2013)
DOI: /j.molcel
Copyright © 2013 Elsevier Inc. Terms and Conditions

2. Figure 1 Molecular Architecture CRISPR-Cas Effector Complexes
(A) Reconstructions of overall shape and architecture of different CRISPR complexes, i.e., the type I Cascade of E. coli resembling a “seahorse” (according to Wiedenheft et al., 2011b), the type III-A CSM complex after fitting a 38 bp DNA duplex to show the potential binding site of a crRNA along its backbone formed by the crescent-shaped molecule Cas7 (Rouillon et al., 2013), and the “sea worm” type III-B Cmr complex (Staals et al., 2013). Segmented regions are colored and labeled to denote proteins Cmr1/Cmr6 (orange), Cmr2 (purple), Cmr3 (green), Cmr4 (alternating light blue and gray), and Cmr5 (red).
(B) Model of eukaryotic Argonaute, the catalytic core of the effector complex RISC. The N-terminal, middle, and PIWI domains form a crescent-shaped base, and the PAZ domain is held above this base via a “stalk” region. This organization creates positively charged grooves that can accommodate an RNA duplex. Structure adopted from (Kuhn and Joshua-Tor, 2013).
Molecular Cell  , 4-7DOI: ( /j.molcel )
Copyright © 2013 Elsevier Inc. Terms and Conditions