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Featured Citations

Convergent and lineage-specific genomic changes shape adaptations in sugar-consuming birds. Osipova E, Ko MC et al. Science. 2026 Feb 26;391(6788):eadt1522.

Ligand-specific activation trajectories dictate GPCR signalling in cells. Thomas R, Jacoby PS et al. Nature. 2026 Feb 26;650(8103):1053–1062.

Cryo-electron microscopic visualization of RAD51 filament assembly and end-capping by XRCC3-RAD51C-RAD51D-XRCC2. Greenhough LA, Galanti L et al. Science. 2026 Feb 26;391(6788):eaea1546.

Termination of the integrated stress response. De Miguel C, Thorkelsson SR et al. Science. 2026 Feb 19;397(6787):eadw5137.

Bacteria deliver a microtubule-binding protein into mammalian cells to promote colonization. Costello MS, Neumann B et al. Science. 2026 Feb 19;391(6787):825-830.

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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.

December 16, 2025

The ChimeraX 1.11 production release is available! See the change log for what's new.

November 21, 2025

The ChimeraX 1.11 release candidate is available – please try it and report any issues. See the change log for what's new. This will be the last release to support Red Hat Enterprise Linux 8 and its derivatives.

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UCSF ChimeraX

UCSF ChimeraX (or simply ChimeraX) is the next-generation molecular visualization program from the Resource for Biocomputing, Visualization, and Informatics (RBVI), following UCSF Chimera. ChimeraX can be downloaded free of charge for academic, government, nonprofit, and personal use. Commercial users, please see ChimeraX commercial licensing.

ChimeraX is developed with support from National Institutes of Health R01-GM129325.

Bluesky logo ChimeraX on Bluesky: @chimerax.ucsf.edu

Feature Highlight

matchmaker superposition screenshot

Matchmaker Superposition

The Matchmaker tool (or matchmaker command) is convenient for superimposing related structures without having to worry about numbering or missing residues. It superimposes proteins or nucleic acids by creating a pairwise sequence alignment, then matching the sequence-aligned residues in 3D. Secondary structure helps guide the sequence alignment for better performance on more distantly related proteins with harder-to-align sequences. By default, the fit is iterated to exclude structurally dissimilar regions and superimpose the most similar parts more closely.

The resulting sequence alignments can be displayed, as in this example of three pectate lyases: PDB 1jta, 1bn8, and 2pec (see the command file peclyases.cxc). In the sequence alignments, residues used in the final fit iteration are enclosed in light orange boxes. RMSD values and other fit statistics are reported in the Log.

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Example Image

potassium channel

Potassium Channel-Calmodulin Complex

KCNQ1 is the pore-forming subunit of a cardiac potassium channel. It binds to calmodulin, and mutations in either of these proteins can cause congenital long QT syndrome, a dangerous propensity for irregular heartbeats. In the image, a structure of the KCNQ1/calmodulin complex (PDB 5vms) has been assembled into the native tetrameric form with the sym command. The view is from the cytoplasmic side, with KCNQ1 shown as surfaces, calmodulin as cartoons, and calcium ions as balls. A pastel palette from ColorBrewer has been used to color the surfaces, darkened with color modify for the cartoons, and “rotated” 45° in hue for the ions. See the command file colormod.cxc.

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