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Recent Citations

A guide to the visual analysis and communication of biomolecular structural data. Johnson GT, Hertig S. Nat Rev Mol Cell Biol. 2014 Oct;15(10):690-8.

Crystal structure of the CRISPR RNA-guided surveillance complex from Escherichia coli. Jackson RN, Golden SM et al. Science. 2014 Sep 19;345(6203):1473-9.

Molecular architecture and mechanism of the anaphase-promoting complex. Chang L, Zhang Z et al. Nature. 2014 Sep 18;513(7518):388-93.

Spatial localization of the Ebola virus glycoprotein mucin-like domain determined by cryo-electron tomography. Tran EE, Simmons JA et al. J Virol. 2014 Sep 15;88(18):10958-62.

Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins. Atherton J, Farabella I et al. eLife. 2014 Sep 10;3:e03680.

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Chimera Search

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August 15, 2014

We are delighted to announce the publication of a new book, Computational and Visualization Techniques for Structural Bioinformatics Using Chimera, written by Forbes J. Burkowski (University of Waterloo).

May 13, 2014

Chimera production release 1.9 is now available. See the release notes for new features since the 1.8 release series.

April 23, 2014

A production release candidate (version 1.9) is now available; please try it and report any problems. See the release notes for changes relative to the previous release.

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UCSF Chimera is a highly extensible program for interactive visualization and analysis of molecular structures and related data, including density maps, supramolecular assemblies, sequence alignments, docking results, trajectories, and conformational ensembles. High-quality images and animations can be generated. Chimera includes complete documentation and several tutorials, and can be downloaded free of charge for academic, government, non-profit, and personal use. Chimera is developed by the Resource for Biocomputing, Visualization, and Informatics, funded by the National Institutes of Health (NIGMS P41-GM103311).

Feature Highlight

Ramachandran plot 1jfuA 1jfu chain A

Ramachandran Plot

Protein backbone angles can be shown in a Ramachandran Plot along with probability contours (green lines) from a reference set of well-determined structures. Each amino acid residue is shown as a dot in a graph of φ vs. ψ, more commonly known as a Ramachandran plot or Ramachandran map. Residues are shown as blue dots, or when selected, as red dots. In the example, all helix residues have been selected. Conversely, clicking a dot in the plot will select the corresponding residue in the structure. When the plot has mouse focus, the cursor position (x = φ, y = ψ) is reported under the plot.

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Gallery Sample


Thermosomes are hollow balls inside which proteins are folded. They are found in the cytosol of eukaryotes and in archaea. Eukaryotic thermosomes have 8 different protein subunits, while archaeal ones are composed of one, two or three different proteins. The one shown from Thermoplasma acidophilum has two distinct proteins colored blue and yellow, each present in 8 copies. The two proteins have 60% sequence identity and are very similar in structure. One monomer is shown as a ribbon. Actin and tubulin are folded by eukaryotic thermosomes.

Protein Data Bank model 1a6d.

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