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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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December 25, 2025
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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 (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.
ChimeraX on Bluesky:
@chimerax.ucsf.edu
Feature Highlight
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.
More features...
Example Image
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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