K2P channel gating mechanisms revealed by structures of TREK-2 and a complex with Prozac. Dong YY, Pike AC et al. Science. 2015 Mar 13;347(6227):1256-1259.
Structure of the F-actin-tropomyosin complex. von der Ecken J, Müller M et al. Nature. 2015 Mar 5;519(7541):114-7.
AAV-expressed eCD4-Ig provides durable protection from multiple SHIV challenges. Gardner MR, Kattenhorn LM et al. Nature. 2015 Mar 5;519(7541):87-91.
Sparse networks of directly coupled, polymorphic, and functional side chains in allosteric proteins. Soltan Ghoraie L, Burkowski F, Zhu M. Proteins. 2015 Mar;83(3):497-516.
Xlink Analyzer: Software for analysis and visualization of cross-linking data in the context of three-dimensional structures. Kosinski J, von Appen A et al. J Struct Biol. 2015 Mar;189(3):177-83.(Previously featured citations...)
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January 9, 2015
Chimera production release 1.10.1 is now available. 64-bit builds are recommended for all capable platforms, and the 1.10 series will be the last to support OS X 10.6 and 10.7. See the release notes for details.
November 5, 2014
Chimera production release 1.10 is now available. 64-bit builds are recommended for all capable platforms, and v1.10 will be the last to support OS X 10.6 and 10.7. See the release notes for what's new.
October 23, 2014
A production release candidate (v1.10) is available; please try it and report any problems. 64-bit builds are now recommended for all capable platforms, and v1.10 will be the last to support OS X 10.6 and 10.7. See the release notes for what's new.(Previous news...)
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).
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.
The image shows interactions of the delta-1 loop with the rest of hepatitis C virus RNA-dependent RNA polymerase (Protein Data Bank entry 1quv). Loop residues in contact with the rest of the structure (van der Waals overlap ≥ 0.01 Å) are displayed as sticks; interacting surface atoms are shown as red patches. (More samples...)