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Featured Citations

Integrase anchors viral RNA to the HIV-1 capsid interior. Singer MR, Li Z et al. Nature. 2026 Apr 23;652(8111):1068–1075.

The E3 ubiquitin ligase mechanism specifying targeted microRNA degradation. Farnung J, Slobodyanyuk E et al. Nature. 2026 Apr 16;652(8110):784–793.

Non-equilibrium snapshots of ligand efficacy at the μ-opioid receptor. Robertson MJ, Modak A et al. Nature. 2026 Apr 16;652(8110):794–802.

The dynamic basis of G-protein recognition and activation by a GPCR. Kobayashi K, Kawakami K et al. Nature. 2026 Apr 16;652(8110):812–821.

Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape. Springstein BL, Javoor MG et al. Science. 2026 Apr 16;392(6795):eaea6343.

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News

December 25, 2025

computer generated image
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.

Previous news...

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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

membrane protein with lipophilicity coloring

Coloring by Molecular Lipophilicity Potential

Molecular lipophilicity potential (MLP) can be calculated for a protein and displayed with surface coloring using the command mlp or the Molecule Display icon computer generated image. The image shows the photosynthetic reaction center from a purple sulfur bacterium, with MLP coloring on the molecular surface and membrane boundaries from OPM (Orientations of Proteins in Membranes entry 1eys). Blue and red balls represent the cytoplasmic and periplasmic sides of the bacterial inner membrane, respectively. Parts of the L, M, and H chains span the membrane, whereas the cytochrome subunit sits on the periplasmic side, at the top. The surface coloring ranges from dark goldenrod for the most hydrophobic potentials, through white, to dark cyan for the most hydrophilic. Ligands including lipid, detergent, heme, and various other cofactors are shown as purple surfaces.

For image setup after the structure from OPM has been opened, see the command file mlp.cxc.

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Example Image

CaM-CaMKI peptide

Calmodulin and Target Peptide

Calmodulin (CaM) acts as a calcium sensor. When its four Ca++ sites are fully occupied, it binds and modulates the activity of various downstream proteins, including CaM-dependent protein kinase I (CaMKI). Here, a complex between CaM and its target peptide from CaMKI (PDB 1mxe) is shown with cartoons, a transparent molecular surface, silhouette outlines, and light soft ambient occlusion. (If you prefer a less smudgy/rustic appearance, try using light gentle instead.) For image setup other than positioning, see the command file cam.cxc.

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