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Cryo-EM structure of the vaccinia virus entry fusion complex reveals a multicomponent fusion machinery. Lin CS, Li CA et al. Sci Adv. 2026 Jan 16;12(3):eaec0254.
Toward community-driven visual proteomics with large-scale cryo-electron tomography of Chlamydomonas reinhardtii. Kelley R, Khavnekar S et al. Mol Cell. 2026 Jan 8;86(1):213-230.e7.
Structural insights into the activation mechanism of the human metabolite receptor HCAR1. Gao M, Zang S et al. Sci Signal. 2026 Jan 6;19(919):eadw1483.
Crystal structure of Methanococcus jannaschii dihydroorotase with substrate bound. Vitali J, Nix JC et al. Acta Crystallogr F Struct Biol Commun. 2026 Jan 1;82(Pt 1):23-31.
Correlation between solvation free energy and solute-solvent interaction energy in energy representation theory. Maruyama Y, Matubayasi N. J Phys Chem B. 2025 Dec 25;129(51):13230-13241.
Previously featured citations...Chimera Search
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December 25, 2025
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September 22, 2025
Mac users may wish to defer upgrading to MacOS Tahoe. Currently on that OS the Chimera graphics window is shifted so that it covers the command and status lines.
March 6, 2025
Chimera production release 1.19 is now available, fixing the ability to fetch structures from the PDB (1.19 release notes).
Previous news...Upcoming Events
UCSF Chimera is a program for the interactive visualization and analysis of molecular structures and related data, including density maps, trajectories, and sequence alignments. It is available free of charge for noncommercial use. Commercial users, please see Chimera commercial licensing.
We encourage Chimera users to try ChimeraX for much better performance with large structures, as well as other major advantages and completely new features in addition to nearly all the capabilities of Chimera (details...).
Chimera is no longer under active development. Chimera development was supported by a grant from the National Institutes of Health (P41-GM103311) that ended in 2018.
Feature Highlight
There are several ways to superimpose structures in Chimera:
•
MatchMaker performs a fit after automatically identifying
which residues should be paired.
Pairing uses both sequence and secondary structure,
allowing similar structures to be superimposed even when
their sequence similarity is low to undetectable.
The figure shows five distantly related proteins
(pairwise sequence identities <25%) from the
SCOP WD40 superfamily before and after
MatchMaker superposition with default parameters.
•
Structures can be matched
using a pre-existing sequence alignment.
•
The exact atoms to pair can be specified with the
match command.
This works on any type of structure, while the preceding methods
apply only to peptide and nucleotide chains.
•
Structures can be superimposed manually by
activating/deactivating them for motion and
using the mouse.
Gallery Sample
Mutations that inactivate the tumor suppressor p53 are found in over 50% of human cancers, and most of the cancer-associated mutations are within its DNA-binding domain. The image shows a tetramer of the p53 DNA-binding domain complexed with DNA (Protein Data Bank entry 2ac0). The tetramer subunits are shown as light blue, green, orange, and yellow ribbons, with red spheres marking several major "hot spots" of mutation. The DNA is shown in purple and blue. (More samples...)
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