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Recent Citations
Regulation of STING activation by phosphoinositide and cholesterol. Li J, Tan JX et al. Nature. 2026 Apr 9;652(8109):499–507.
eT 2.0: An efficient open-source molecular electronic structure program. Folkestad SD, Kjønstad EF et al. J Chem Phys. 2026 Apr 7;164(13):132501.
The Erlin1/2 complex is a dynamic scaffold for membrane microdomain assembly on the endoplasmic reticulum. Yan L, Xu Z et al. Mol Cell. 2026 Apr 2;86(7):1362-1376.e5.
Microtubules guide Aurora B substrate geometries for accurate chromosome segregation. Niu Y, DeLuca KF et al. Sci Adv. 2026 Mar 27;12(13):eaea2112.
Discovery and cryoEM structure of FPM13, a periplasmic metalloprotein unique to Francisella. Clemens DL, Lee BY et al. PLoS Pathog. 2026 Mar 27;22(3):e1014024.
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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).
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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
Large ribosomal RNA is shown with individual bases depicted using solvent excluded molecular surfaces. Bases A, C, G, U are colored red, yellow, green, and blue. The surfaces were made with the Chimera multiscale tool in combination with the nucleic acid blobs plug-in. The image was raytraced using POVray.
Protein Data Bank model 1s72.
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