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Recent Citations

The 4-electron cleavage of a N═N double bond by a trimetallic TiNi2 complex. Dunn PL, Chatterjee S et al. Inorg Chem. 2019 Sep 3;58(17):11762-11772.

The central role of the tail in switching off 10S myosin II activity. Yang S, Lee KH et al. J Gen Physiol. 2019 Sep 2;151(9):1081-1093.

Methods for merging data sets in electron cryo-microscopy. Wilkinson ME, Kumar A, Casañal A. Acta Crystallogr D Struct Biol. 2019 Sep 1;75(Pt 9):782-791.

Current understanding of the role of neuronal calcium sensor 1 in neurological disorders. Bandura J, Feng ZP. Mol Neurobiol. 2019 Sep;56(9):6080-6094.

Atomic structure of the Epstein-Barr virus portal. Machón C, Fàbrega-Ferrer M et al. Nat Commun. 2019 Aug 29;10(1):3891.

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November 17, 2018

Chimera production release 1.13.1 is now available; see the release notes for what's new. The Mac version requires OS 10.10 or later.

October 22, 2018

Mac users: the 1.13.1 release candidate and recent daily builds contain a fix for Mojave (OS 10.14). These versions require OS 10.10 or later.

September 21, 2018

Mac users are advised to hold off upgrading to Mojave until we find a fix for Chimera buttons not being shown until the windows containing them are resized.

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

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

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

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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