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SPARC: a structural pathogenicity algorithm for risk classification of hERG variants. Chatelain FC, de Oliveira BR et al. Europace. 2026 Feb 3;28(2):euaf327.

Cryo-EM structure of the vaccinia virus entry fusion complex reveals a multicomponent fusion machinery. Lin CS, Li CA et al. Sci Adv. 2026 Jan 16;12(3):eaec0254.

Toward community-driven visual proteomics with large-scale cryo-electron tomography of Chlamydomonas reinhardtii. Kelley R, Khavnekar S et al. Mol Cell. 2026 Jan 8;86(1):213-230.e7.

Structural insights into the activation mechanism of the human metabolite receptor HCAR1. Gao M, Zang S et al. Sci Signal. 2026 Jan 6;19(919):eadw1483.

Crystal structure of Methanococcus jannaschii dihydroorotase with substrate bound. Vitali J, Nix JC et al. Acta Crystallogr F Struct Biol Commun. 2026 Jan 1;82(Pt 1):23-31.

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December 25, 2025

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The RBVI wishes you a safe and happy holiday season! See our 2025 card and the gallery of previous cards back to 1985.

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.

March 6, 2025

Chimera production release 1.19 is now available, fixing the ability to fetch structures from the PDB (1.19 release notes).

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Please note that UCSF Chimera is legacy software that is no longer being developed or supported. Users are strongly encouraged to try UCSF ChimeraX, which is under active development.
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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

sequence alignment structure

Sequence Viewer

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,

  • mousing over a residue in the sequence shows its structure residue number
  • selecting in the sequence selects residues in the structure(s) and vice versa
  • structures can be superimposed using the sequence alignment
Various measures of sequence conservation and structural variation (RMSD) can be computed and shown above the sequences as histograms, and on the structures with color or worm radius. Secondary structure elements can be depicted as colored boxes or regions on the alignment. Regions can also be created by hand.

(More features...)

Gallery Sample

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Sliced Potassium Channel

Potassium channel (Protein Data Bank entry 1bl8) on a dark slate blue background with potassium ions shown in firebrick. The channel is comprised of four chains. Each chain has been rainbow-colored from blue at the N-terminus to red at the C-terminus, but only the surface of the channel is shown. The surface has been sliced with a per-model clipping plane. The surface cap color is plum except with opacity set to 0.8. The shininess and brightness have been set to 128 and 8, respectively, and the lights on the scene have been moved from their default positions. The subdivision quality (related to the smoothness of the spherical ions) is 5.0, and the molecular surface was computed with probe radius and vertex density set to 1.0 and 6.0, respectively. (More samples...)


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