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Recent Citations
Mechanism of Tc toxin action revealed in molecular detail. Meusch D, Gatsogiannis C et al. Nature. 2014 Apr 3;508(7494):61-5.
Structural basis for pure antagonism of integrin αVβ3 by a high-affinity form of fibronectin. Van Agthoven JF, Xiong JP et al. Nat Struct Mol Biol. 2014 Apr;21(4):383-8.
Structure of the yeast mitochondrial large ribosomal subunit. Amunts A, Brown A et al. Science. 2014 Mar 28;343(6178):1485-9.
Patches of disorganization in the neocortex of children with autism. Stoner R, Chow ML et al. N Engl J Med. 2014 Mar 27;370(13):1209-19.
Molecular basis for erythromycin-dependent ribosome stalling during translation of the ErmBL leader peptide. Arenz S, Ramu H et al. Nat Commun. 2014 Mar 24;5:3501.
(Previously featured citations...)Chimera Search
Google™ SearchNews
October 31, 2013
Chimera production release 1.8.1 is now available. Changes since 1.8 are mainly to fix problems with Mac OS X 10.9 (Mavericks). See the release notes for further details and for a list of new features since the 1.7 release.
June 7, 2013
Chimera production release 1.8 is now available. See the release notes for new features since the 1.7 release.
April 18, 2013
A production release candidate (version 1.8) is now available; please try it and report any problems. See the release notes for changes relative to the previous release.
(Previous news...)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, 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
Gallery Sample
Potassium channel (Protein Data Bank entry 1bl8) on a dark slate blue background with potassium ions shown in firebrick. The channel is comprised of four chains. Each chain has been rainbow-colored from blue at the N-terminus to red at the C-terminus, but only the surface of the channel is shown. The surface has been sliced with a per-model clipping plane. The surface cap color is plum except with opacity set to 0.8. The shininess and brightness have been set to 128 and 8, respectively, and the lights on the scene have been moved from their default positions. The subdivision quality (related to the smoothness of the spherical ions) is 5.0, and the molecular surface was computed with probe radius and vertex density set to 1.0 and 6.0, respectively. (More samples...)