The CaMKII holoenzyme structure in activation-competent conformations. Myers JB, Zaegel V et al. Nat Commun. 2017 Jun 7;8:15742.
Structural basis for antibody-mediated neutralization of Lassa virus. Hastie KM, Zandonatti MA et al. Science. 2017 Jun 2;356(6341):923-928.
Cryo-electron microscopy of chromatin biology. Wilson MD, Costa A. Acta Crystallogr D Struct Biol. 2017 Jun 1;73(Pt 6):541-548.
Halogenated ether, alcohol, and alkane anesthetics activate TASK-3 tandem pore potassium channels likely through a common mechanism. Luethy A, Boghosian JD et al. Mol Pharmacol. 2017 Jun;91(6):620-629.
Phase-plate cryo-EM structure of a class B GPCR-G-protein complex. Liang YL, Khoshouei M et al. Nature. 2017 Jun 1;546(7656):118-123.(Previously featured citations...)
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December 2, 2016
September 24, 2016
Production release candidate (version 1.11.2) is available, superseding 1.11.1. The new version has been updated to work with changes in NCBI Blast (see release notes). Please try it and report any problems.
August 27, 2016
A production release candidate (version 1.11.1) is now available. Please try it and report any problems. See the release notes for what's been fixed since 1.11. The 1.11 release series will be the last to support 32-bit builds.(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, nonprofit, and personal use. Chimera is developed by the Resource for Biocomputing, Visualization, and Informatics (RBVI), funded by the National Institutes of Health (NIGMS P41-GM103311).
UCSF ChimeraX (or simply ChimeraX) is the next-generation molecular visualization program from the RBVI, following UCSF Chimera.
Mutations that inactivate the tumor suppressor p53 are found in over 50% of human cancers, and most of the cancer-associated mutations are within its DNA-binding domain. The image shows a tetramer of the p53 DNA-binding domain complexed with DNA (Protein Data Bank entry 2ac0). The tetramer subunits are shown as light blue, green, orange, and yellow ribbons, with red spheres marking several major "hot spots" of mutation. The DNA is shown in purple and blue. (More samples...)