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Featured Citations

Vaccination generates broadly cross-neutralizing antibodies to the HIV Env apex. Guenaga J, Ádori M et al. Nature. 2026 Jun 18;654(8119):777–785.

Induction of broadly neutralizing HIV antibodies by a two-step mechanism informs vaccine design. Skelly AN, Gristick HB et al. Science. 2026 Jun 18;392(6804):eaec6396.

Cryo-EM reveals a right-handed double-helix dimer architecture of PCDH15. Liang X, Pathak R et al. Proc Natl Acad Sci USA. 2026 Jun 16;123(24):e2607573123.

Structure of the mouse cytoplasmic lattice. Chi P, Wang X et al. Nature. 2026 Jun 10;654(8118):523–531.

Pervasive and programmed nucleosome distortion on single chromatin fibres. Yang MG, Richter HJ et al. Nature. 2026 Jun 10;654(8118):513–522.

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News

June 11, 2026

The ChimeraX 1.12 production release is available! See the change log for what's new.

May 7, 2026

The ChimeraX 1.12 release candidate is available – please try it and report any issues. See the change log for what's new.

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.

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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

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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