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Featured Citations

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.

DNA damage drives antigen diversification in Trypanosoma brucei. Smith JE, Wang KJ et al. Nature. 2026 Jun 4;654(8117):219–228.

Ultrastructure of dopaminergic varicosities revealed by cryo-correlative light and electron microscopy. Lycas MD, Morado DR et al. J Cell Biol. 2026 Jun 1;225(6):e202503059.

Selective autophagy fine-tunes plant immunity to promote cell survival during viral infection. Clavel M, Bianchi A et al. Science. 2026 May 28;392(6801):eadu9554.

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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

THRβ and binding-site rotamers rotamer list dialog

Rotamers and Swapaa Virtual Mutation

Rotamers is an interface for showing amino acid sidechain rotamers and optionally replacing the original sidechain, also implemented as the swapaa command. The rotamers can be shown all at once, as in the figure, or individually by choosing rows in the dialog.

The figure shows binding-site residues of the thyroid hormone receptor β with hormone bound, PDB 3gws. Rotamers for the hormone-resistance mutations N331H and L346R are shown as partially transparent sticks, with H-bonds (light blue dashed line) and clashes (light purple dashed lines) calculated for the histidine rotamers at position 331. The rotamer-list dialog for this position is also shown. Command script rotamers.cxc contains the initial, noninteractive part of the setup.

These mutations are described in Cardoso et al., Endocrine (2020). Although one histidine rotamer may be able to form the same pocket-stabilizing H-bond as the wild-type asparagine, it also clashes with several atoms (third row in the dialog). H-bonds and clashes are not shown for the arginine rotamers at 346, but they all clash significantly with the hormone and/or other pocket atoms.

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Example Image

cyclodextrin pore

Cyclodextrin Pore

The outer-membrane protein CymA admits bulky molecules into the periplasmic space of Klebsiella oxytoca. Here, CymA (PDB 4d5d chain A) is depicted in a style reminiscent of a diagnostic X-ray, with transparent molecular surface and β-strand “ribs” in white. The protein has ingested α-cyclodextrin (top) and β-cyclodextrin (bottom), bound at the entry site and near the exit, respectively. Cyclodextrin carbon atoms are shown in blue-gray and oxygen atoms in brick red. For image setup, see the command file xray.cxc.

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