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. Author manuscript; available in PMC: 2014 Mar 1.
Published in final edited form as: Crit Rev Biochem Mol Biol. 2012 Dec 13;48(2):89–97. doi: 10.3109/10409238.2012.742856

Figure 4.

Figure 4

The flexibility of cullin from the molecular dynamics simulations is validated by electron microscopy. (a) The Cull1-Rbx1 components of SCF are displayed side-by-side with the average cryo-EM map of Ltn1. (b) The random-conical tilt (RCT) reconstruction of one conformer of Cul1-Rbx1 complex identified by negative stain EM at ~40Å resolution. (c) RCT reconstruction of the second conformer of Cul1-Rbx1 complex identified by negative stain EM at ~40Å resolution. The Cul1-Rbx1 complex structures from snapshots taken from the MD simulation are fit to the first (e) and second (f) EM conformer, respectively. (d) Overlay of the two conformers identified by EM, showing apparent flexibility in the vicinity of the region between the second and third cullin repeat. (g) The Cul1-Rbx1 crystal structure is overlaid on a simulated 40Å electron density map, so as to show a more accurate comparison to the low-resolution EM maps. (Dr. Dmitry Lyumkis from the Scripps Institute, personal communication; Dmitry Lyumkis, Selom K. Doamekpor, Mario H. Bengtson, Joong-Won Lee, Tasha B. Toro, Matthew D. Petroski, Christopher D. Lima, Clinton S. Potter, Bridget Carragher, and Claudio A. P. Joazeiro, manuscript submitted).