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Plug-in strategy for resistance engineering inspired by potato NLRome. Wang L, Li H et al. Nature. 2026 Jan 8;649(8096):396–405.

Deep contrastive learning enables genome-wide virtual screening. Jia Y, Gao B et al. Science. 2026 Jan 8;391(6781):eads9530.

Recurrent acquisition of nuclease-protease pairs in antiviral immunity. Tuck OT, Hu JJ et al. Science. 2026 Jan 8;391(6781):195-201.

Asynchronous subunit transitions prime acetylcholine receptor activation. Thompson MJ, Tessier CJG et al. Science. 2026 Jan 1;391(6780):eadw1264.

Mechanism of cotranslational modification of histones H2A and H4 by MetAP1 and NatD. Yudin D, Jaskolowski M et al. Sci Adv. 2025 Dec 19;11(51):eaeb1017.

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News

December 25, 2025

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

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 . 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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