The native structure of the assembled matrix protein 1 of influenza A virus. Peukes J, Xiong X et al. Nature. 2020 Nov 19;587(7834):495-498.
Structural basis of GPBAR activation and bile acid recognition. Yang F, Mao C et al. Nature. 2020 Nov 19;587(7834):499-504.
Molecular mechanism for rotational switching of the bacterial flagellar motor. Chang Y, Zhang K et al. Nat Struct Mol Biol. 2020 Nov;27(11):1041-1047.
The coupling mechanism of mammalian respiratory complex I. Kampjut D, Sazanov LA. Science. 2020 Oct 30;370(6516):eabc4209.
In-cell architecture of the nuclear pore and snapshots of its turnover. Allegretti M, Zimmerli CE et al. Nature. 2020 Oct 29;586(7831):796-800.(Previously featured citations...)
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UCSF Chimera is a program for the interactive visualization and analysis of molecular structures and related data, including density maps, trajectories, and sequence alignments. High-quality images and animations can be generated. Chimera includes complete documentation and is free of charge for academic, government, nonprofit, and personal use. Commercial users, please see Chimera commercial licensing.
Chimera development was supported by the National Institutes of Health (P41-GM103311).
UCSF ChimeraX is the next-generation molecular visualization program from the RBVI, following UCSF Chimera. We encourage Chimera users to try ChimeraX for much better performance with large structures, as well as other major advantages. ChimeraX replaces a significant subset of Chimera features, includes several completely new features, and is under active development. Users may certainly choose to use both programs, and it is fine to have both installed.
A simple, line-drawing-like appearance can be achieved by combining black silhouette edges with flat, ambient-only lighting. The image at left of a small molecule in ball-and-stick style can be generated with a few Chimera commands. The same visual effects can be applied to ribbons and other representations, as shown in Neuraminidase Flowers and other Image Gallery entries.(More features...)
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...)
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