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Recent Citations

Structures of Ostα/β reveal a unique fold and bile acid transport mechanism. Yang X, Cui N et al. Nature. 2026 Mar 5;651(8104):260–267.

Structure and mechanism of the human bile acid transporter OSTα-OSTβ. Wang K, Fan J et al. Nature. 2026 Mar 5;651(8104):251–259

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.

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News

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

Ramachandran plot 1jfuA 1jfu chain A

Ramachandran Plot

Protein backbone angles can be shown in a Ramachandran Plot along with probability contours (green lines) from a reference set of well-determined structures. Each amino acid residue is shown as a dot in a graph of φ vs. ψ, more commonly known as a Ramachandran plot or Ramachandran map. Residues are shown as blue dots, or when selected, as red dots. In the example, all helix residues have been selected. Conversely, clicking a dot in the plot will select the corresponding residue in the structure. When the plot has mouse focus, the cursor position (x = φ, y = ψ) is reported under the plot.

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Gallery Sample

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Molecular Bracelet

Eukaryotic initiation factor (eIF) complex (from Protein Data Bank entry 1rf8) in which eIF4E, shown with blue ribbons, is completely encircled by eIF4G, shown with yellow ribbons and red molecular surface (image creation details). (More samples...)


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