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Recent Citations

Cryo-EM structure of the αvβ8 integrin reveals a mechanism for stabilizing integrin extension. Cormier A, Campbell MG et al. Nat Struct Mol Biol. 2018 Aug;25(8):698-704.

A new HIV-1 Rev structure optimizes interaction with target RNA (RRE) for nuclear export. Watts NR, Eren E et al. J Struct Biol. 2018 Aug;203(2):102-108.

Expanded coverage of the 26S proteasome conformational landscape reveals mechanisms of peptidase gating. Eisele MR, Reed RG et al. Cell Rep. 2018 Jul 31;24(5):1301-1315.e5.

Cryo-EM structures of fungal and metazoan mitochondrial calcium uniporters. Baradaran R, Wang C et al. Nature. 2018 Jul 26;559(7715):580-584.

HIV-1 Nefs are cargo-sensitive AP-1 trimerization switches in tetherin downregulation. Morris KL, Buffalo CZ et al. Cell. 2018 Jul 26;174(3):659-671.e14.

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Chimera Search

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News

July 3, 2018

Chimera production release 1.13 is now available. See the release notes for what's new.

June 2, 2018

A production release candidate (version 1.13) is available; please try it and report any problems. See the release notes for what's new.

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.

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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), 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

conservation coloring

Coloring by Conservation

A structure can be colored to show attributes such as residue conservation. Opening a sequence alignment in Chimera shows it in Multalign Viewer and automatically associates sequences with structures as appropriate. Residues of alignment-associated structures are assigned conservation values; available measures include entropy, variability, and sum-of-pairs. The figure was created using the PFAM Carb_anhydrase seed alignment PF00194_seed.slx (see image) and includes 2D labels and a color key. See also: mapping sequence conservation

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Gallery Sample

Wasabi Receptor

The image shows the structure of the human TRPA1 ion channel (wasabi receptor) determined by electron cryo-microscopy, Protein Data Bank entry 3j9p. The four subunits of the tetramer are shown as ribbons in different colors over a dark-to-light gradient background. (More samples...)