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Recent Citations

Structural basis of the nucleosome transition during RNA polymerase II passage. Kujirai T, Ehara H et al. Science. 2018 Nov 2;362(6414):595-598.

Cross-linked peptide identification: A computational forest of algorithms. Yılmaz Ş, Shiferaw GA et al. Mass Spectrom Rev. 2018 Nov;37(6):738-749.

Conformational flexibility of pore loop-1 gives insights into substrate translocation by the AAA+ protease FtsH. Uthoff M, Baumann U. J Struct Biol. 2018 Nov;204(2):199-206.

Hierarchical organization endows the kinase domain with regulatory plasticity. Creixell P, Pandey JP et al. Cell Syst. 2018 Oct 24;7(4):371-383.e4.

The structure and dynamics of C. elegans tubulin reveals the mechanistic basis of microtubule growth. Chaaban S, Jariwala S et al. Dev Cell. 2018 Oct 22;47(2):191-204.e8.

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News

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.

July 3, 2018

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

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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

Sliced Potassium Channel

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...)


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