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. 2009 Oct 2;5(10):e1000526. doi: 10.1371/journal.pcbi.1000526

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Lu, Liang.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Side view for the R″ state (left), top view (upper right) and side view (lower right) for the T, R and R″ state (pdb ids , and , respectively). The GroEL-GroES chaperone complex is large, consisting of 8,015 residues in the resolved structure, with 14 and 7 chains in the homo-oligemeric GroEL and GroES subunits, respectively. Each chain in the GroEL structure contains three domains: the E (equatorial) domain, the I (intermediate) domain, and the A (apical) domain, reflecting their respective spatial positions in the GroEL-GroES chaperone complex.

Inline graphic — Side view for the R″ state (left), top view (upper right) and side view (lower right) for the T, R and R″ state (pdb ids , and , respectively). The GroEL-GroES chaperone complex is large, consisting of 8,015 residues in the resolved structure, with 14 and 7 chains in the homo-oligemeric GroEL and GroES subunits, respectively. Each chain in the GroEL structure contains three domains: the E (equatorial) domain, the I (intermediate) domain, and the A (apical) domain, reflecting their respective spatial positions in the GroEL-GroES chaperone complex.