Mechanistic insights into the recycling machine of the SNARE complex. Zhao M, Wu S et al. Nature. 2015 Feb 2;518(7537):61-7.
Ring closure activates yeast γTuRC for species-specific microtubule nucleation. Kollman JM, Greenberg CH et al. Nat Struct Mol Biol. 2015 Feb;22(2):132-137.
De novo design of an RNA tile that self-assembles into a homo-octameric nanoprism. Yu J, Liu Z et al. Nat Commun. 2015 Jan 30;6:5724.
A molecular census of 26S proteasomes in intact neurons. Asano S, Fukuda Y et al. Science. 2015 Jan 23;347(6220):439-42.
Structure of the immature HIV-1 capsid in intact virus particles at 8.8 Å resolution. Schur FK, Hagen WJ et al. Nature. 2015 Jan 22;517(7535):505-8.(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).
The default ribbon path is a smooth bspline (semitransparent tan in the figure), which can diverge from the true positions of the backbone atoms (α-carbons shown as gray balls). A cardinal spline allows tracking the backbone more closely. Without smoothing (light blue), it follows the α-carbons exactly, or it can be combined with some “compromise” smoothing of strand and/or coil. Ribbon spline options can be set with the ribspline command or in the molecule model attributes.(More features...)
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...)