Journal: Chemistry and physics of lipids

Article Title: Single-particle cryo-EM studies of transmembrane proteins in SMA copolymer nanodiscs

doi: 10.1016/j.chemphyslip.2019.03.007

Figure Lengend Snippet: Cryo-EM of the alternative complex III: cyt c oxidase supercomplex in SMA nanodiscs. A, 3D reconstruction of the supercomplex. The ACIII is colored in blue while the cyt c oxidase is colored in yellow. Also shown is a smoothed transparent surface of the SMA nanodisc at a lower density value. This panel has been reproduced with permission from Springer Nature. B, 3D reconstruction of the supercomplex colored by local resolution in angstrom.

Article Snippet: Nevertheless, the configuration of ACIII: cyt c oxidase supercomplex is compatible with an efficient electron-channeling mechanism involving the tethered water-soluble cyt c from ActA as the electron carrier. fig ft0 fig mode=article f1 fig/graphic|fig/alternatives/graphic mode="anchored" m1 Open in a separate window Figure 6. caption a7 Lipids resolved in the cryo-EM ACIII structure.

Techniques: Cryo-EM Sample Prep

Journal: Chemistry and physics of lipids

Article Title: Single-particle cryo-EM studies of transmembrane proteins in SMA copolymer nanodiscs

doi: 10.1016/j.chemphyslip.2019.03.007

Figure Lengend Snippet: Structure of the alternative complex III. A, 3D reconstruction of the ACIII colored by subunit. In addition to the six known subunits (ActA to ActF) from the ACIII operon, two small transmembrane peptides ActX and ActY are observed. B, Cartoon representation of the de novo structure of the ACIII colored by subunit. ActX and ActY are not included. Both panels have been modified with permission from Springer Nature.

Article Snippet: Nevertheless, the configuration of ACIII: cyt c oxidase supercomplex is compatible with an efficient electron-channeling mechanism involving the tethered water-soluble cyt c from ActA as the electron carrier. fig ft0 fig mode=article f1 fig/graphic|fig/alternatives/graphic mode="anchored" m1 Open in a separate window Figure 6. caption a7 Lipids resolved in the cryo-EM ACIII structure.

Techniques: Modification

Journal: Chemistry and physics of lipids

Article Title: Single-particle cryo-EM studies of transmembrane proteins in SMA copolymer nanodiscs

doi: 10.1016/j.chemphyslip.2019.03.007

Figure Lengend Snippet: Lipids resolved in the cryo-EM ACIII structure. Four lipid molecules are resolved at the cytoplasmic interface between ActC and ActF. Besides, two lipid molecules clustered near the triacylated cysteine from ActB, right above the proposed menaquinone entry pathway. This figure has been reproduced with permission from Springer Nature.

Article Snippet: Nevertheless, the configuration of ACIII: cyt c oxidase supercomplex is compatible with an efficient electron-channeling mechanism involving the tethered water-soluble cyt c from ActA as the electron carrier. fig ft0 fig mode=article f1 fig/graphic|fig/alternatives/graphic mode="anchored" m1 Open in a separate window Figure 6. caption a7 Lipids resolved in the cryo-EM ACIII structure.

Techniques: Cryo-EM Sample Prep

Journal: Chemistry and physics of lipids

Article Title: Single-particle cryo-EM studies of transmembrane proteins in SMA copolymer nanodiscs

doi: 10.1016/j.chemphyslip.2019.03.007

Figure Lengend Snippet: Cryo-EM of the alternative complex III: cyt c oxidase supercomplex in SMA nanodiscs. A, 3D reconstruction of the supercomplex. The ACIII is colored in blue while the cyt c oxidase is colored in yellow. Also shown is a smoothed transparent surface of the SMA nanodisc at a lower density value. This panel has been reproduced with permission from Springer Nature. B, 3D reconstruction of the supercomplex colored by local resolution in angstrom.

Article Snippet: Only the portion of the cyt c oxidase component of the supercomplex that is near the interface of ACIII is well resolved, but a complete model of supercomplex can be assembled from the cryoEM data by using the existing X-ray structure of related cyt c oxidases.

Techniques: Cryo-EM Sample Prep