Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2024 Jul 1;31(12):1848–1858. doi: 10.1038/s41594-024-01352-0

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Extended Data Fig. 4 — (a) Representative 2D class averages from the mtHsp60^ATP-mtHsp10 dataset. Scale bar equals 100 Å. (b) Cryo-EM processing workflow for structures obtained from the mtHsp60^ATP-mtHsp10 dataset. The mask used for subsequent focused classification is shown (transparent blue) on the consensus D7 refinement. (c) Sharpened map and model for the asymmetric unit of the mtHsp60^ATP-mtHsp10 consensus structure. (d) Overlay of consensus models for mtHsp60^ATP and mtHsp60^ATP-mtHsp10 structures, showing identical equatorial and intermediate domain conformations but a large upward apical domain rotation. (e) Model of the mtHsp10 mobile loop and associated mtHsp60 apical domain in the mtHsp60^ATP-mtHsp10 consensus map, showing interaction of conserved hydrophobic residues with apical domain helices H and I. (f) Coulombic potential maps of protomers of mtHsp60 apo, mtHsp60^ATP, and mtHsp60^ATP-mtHsp10 consensus structures, showing increased negative charge in the inward-facing regions of mtHsp60^ATP-mtHsp10. (g) Overlay of consensus models for mtHsp60^ATP and mtHsp60^ATP-mtHsp10 structures, showing highly similar inter-ring conformations.