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An electron transfer path connects subunits of a mycobacterial respiratory supercomplex. Gong H, Li J et al. Science. 2018 Nov 30;362(6418). pii: eaat8923.

Folding pathway of an Ig domain is conserved on and off the ribosome. Tian P, Steward A et al. Proc Natl Acad Sci USA. 2018 Nov 27;115(48):E11284-E11293.

Tracing whale myoglobin evolution by resurrecting ancient proteins. Isogai Y, Imamura H et al. Sci Rep. 2018 Nov 15;8(1):16883.

Conformational transitions of the serotonin 5-HT3 receptor. Polovinkin L, Hassaine G et al. Nature. 2018 Nov 8;563(7730):275-279.

Germline VRC01 antibody recognition of a modified clade C HIV-1 envelope trimer and a glycosylated HIV-1 gp120 core. Borst AJ, Weidle CE et al. eLife. 2018 Nov 7;7. pii: e37688.

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News

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

structure-based sequence alignment superimposed structures

Structure-Based Sequence Alignment

Given two or more superimposed structures, Match→Align creates a corresponding sequence alignment. The user specifies a distance cutoff for residues allowed to be in the same column of the output alignment. In proteins, the distances are measured between α-carbons. The method is independent of residue types and how the structures were superimposed.
The figure shows a superposition from MatchMaker of five proteins from the SCOP WD40 superfamily and a corresponding sequence alignment from Match→Align, automatically shown in Multalign Viewer. In the sequence alignment, light green and yellow boxes indicate strands and helices, while the headers RMSD and Conservation show spatial and sequence conservation, respectively.

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Gallery Sample

Clathrin

This image of a clathrin cage uses flat shading and edge highlighting. It is a copy of a PDB molecule of the month image made by Graham Johnson and Dave Goodsell. David Goodsell pioneered this visualization style. This image was made with the Multiscale tool, silhouette edging, and surface lighting turned off.

Protein Data Bank model 1xi4.

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