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Cryo-electron microscopy structures of human cone visual pigments. Peng Q, Li J et al. Science. 2026 Jun 25;392(6805):eadz8141.
Steric hindrance of antibody binding in an Omicron spike fusion intermediate. Bao Z, Liu Z et al. Nature. 2026 Jun 18;654(8119):762–770.
Structural basis of fungal β-1,3-glucan synthase inhibition by caspofungin. Ren Z, Chhetri A et al. Nature. 2026 Jun 10;654(8118):547–555.
Myosin forces remodel F-actin for mechanosensitive protein recognition. Carl AG, Reynolds MJ et al. Nature. 2026 Jun 4;654(8117):240–249.
A high-throughput selection system for fast-acting covalent protein drugs. Fan Q, Mei J et al. Science. 2026 May 28;392(6801):eadv3081.
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June 25, 2026
Chimera production release 1.20 is now available, fixing problems on Mac OS Tahoe (1.20 release notes).
December 25, 2025
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September 22, 2025
Mac users may wish to defer upgrading to MacOS Tahoe. Currently on that OS the Chimera graphics window is shifted so that it covers the command and status lines.
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UCSF Chimera is a program for the interactive visualization and analysis of molecular structures and related data, including density maps, trajectories, and sequence alignments. It is available free of charge for noncommercial use. Commercial users, please see Chimera commercial licensing.
We encourage Chimera users to try ChimeraX for much better performance with large structures, as well as other major advantages and completely new features in addition to nearly all the capabilities of Chimera (details...).
Chimera is no longer under active development. Chimera development was supported by a grant from the National Institutes of Health (P41-GM103311) that ended in 2018.
Feature Highlight
The Multalign Viewer tool displays individual sequences and multiple sequence alignments. Sequence alignments can be read from external files (several formats) or created by other tools in Chimera. Structures opened in Chimera are automatically associated with sufficiently similar sequences in the alignment. After association,
Gallery Sample
Thermosomes are hollow balls inside which proteins are folded. They are found in the cytosol of eukaryotes and in archaea. Eukaryotic thermosomes have 8 different protein subunits, while archaeal ones are composed of one, two or three different proteins. The one shown from Thermoplasma acidophilum has two distinct proteins colored blue and yellow, each present in 8 copies. The two proteins have 60% sequence identity and are very similar in structure. One monomer is shown as a ribbon. Actin and tubulin are folded by eukaryotic thermosomes.
Protein Data Bank model 1a6d.
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