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Recent Citations

Structural prediction of protein models using distance restraints derived from cross-linking mass spectrometry data. Orbán-Németh Z, Beveridge R et al. Nat Protoc. 2018 Mar;13(3):478-494.

The cryo-electron microscopy structure of huntingtin. Guo Q, Bin Huang et al. Nature. 2018 Mar 1;555(7694):117-120.

A recurrent kinase domain mutation in PRKCA defines chordoid glioma of the third ventricle. Goode B, Mondal G et al. Nat Commun. 2018 Feb 23;9(1):810.

Electron cryo-microscopy structure of Ebola virus nucleoprotein reveals a mechanism for nucleocapsid-like assembly. Su Z, Wu C et al. Cell. 2018 Feb 22;172(5):966-978.e12.

A structural model of a p450-ferredoxin complex from orientation-selective double electron-electron resonance spectroscopy. Bowen AM, Johnson EOD et al. J Am Chem Soc. 2018 Feb 21;140(7):2514-2527.

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Chimera Search

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October 24, 2017

Chimera production release 1.12 is now available (64-bit builds for Windows, Mac, and Linux). See the release notes for details.

September 12, 2017

A production release candidate (version 1.12) is available; please try it and report any problems. See the release notes for what's new.

March 13, 2017

For a nice 3D-printing protocol that uses Chimera, see 3D Printing of Biomolecular Models for Research and Pedagogy by Da Veiga Beltrame, Tyrwhitt-Drake, et al. today in JoVE!

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Upcoming Events

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, nonprofit, and personal use. Chimera is developed by the Resource for Biocomputing, Visualization, and Informatics (RBVI), funded by the National Institutes of Health (NIGMS P41-GM103311).

UCSF ChimeraX (or simply ChimeraX) is the next-generation molecular visualization program from the RBVI, following UCSF Chimera.

Feature Highlight

sidechain rotamers


Amino acid sidechains adopt different conformational states, or rotamers. Rotamers from the Dunbrack backbone-dependent library or the Richardson "penultimate" library can be viewed, evaluated, and incorporated into structures with the Rotamers tool. A residue can be changed into a different conformation of the same type of amino acid or mutated into a different type. Rotamer torsion angles and library probability values are listed in a dialog, along with (optionally) hydrogen bonds, clashes, and agreement with electron density data. Only rotamers chosen in the list are displayed. When a single rotamer is chosen, it can be incorporated into the structure. The image includes 2D labels.

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Gallery Sample

Peroxiredoxin Wreath

Peroxiredoxins are enzymes that help cells cope with stressors such as high levels of reactive oxygen species. The image shows a decameric peroxiredoxin from human red blood cells (Protein Data Bank entry 1qmv), styled as a holiday wreath.

See also the RBVI holiday card gallery.

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