26S Proteasome Lid Rearrangement
The atomic model of the isolated 26S Proteasome lid subcomplex, as determined by cryoEM, shows the rearrangements its subunits undergo upon incorporation into the functional 26S proteasome regulatory particle.

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26S Proteasome Engages Substrate
CryoEM reconstruction of the yeast 26S proteasome, showing the structural rearrangements that the regulatory particle undergoes upon substrate engagement.

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26S Proteasome Architecture
CryoEM reconstruction of the yeast 26S proteasome, showing the spatial arrangement of all subunits within the regulatory particle, including the ubiquitin receptors and the deubiquitinating enzyme.

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Bacteriophage P22 Virion Assembly
This is a cartoon-style interpretation of how the bacteriophage P22 virion assembles. Although this assembly is specific to P22, it also serves as a generalized model for all phage assembly.

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Bacteriophage P22 Tail Machine Assembly
The tail machine is a 2 megadalton structure used by Bacteriophage P22 to infect Salmonella bacteria. This is an interpretation of how it might assemble, based on a cryoEM reconstruction at subnanometer resolution.

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Phage P22 Asymmetric Reconstruction
A dissection of the 3D cryoEM reconstruction of bacteriophage P22 at 17 Angstrom resolution. Since its initial publication in 2006, this structure has been solved to much higher resolutions by several labs.

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Molecular Chaperone GroEL
GroEL is a molecular complex that helps proteins fold properly in E. coli cells, a molecular machine referred to as a chaperone. Due to its size, stability, symmetry, and the fact that is has been studied extensively structurally and functionally, it is an ideal specimen for structural analysis by cryoEM. This is a cryoEM reconstruction of GroEL at about 5 Angstroms resolution.

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