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Structural analysis of full-length SARS-CoV-2 spike protein from an advanced vaccine candidate. Bangaru S, Ozorowski G et al. Science. 2020 Nov 27;370(6520):1089-1094.

Ultrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms. Tortorici MA, Beltramello M et al. Science. 2020 Nov 20;370(6519):950-957.

Structure of the human sodium leak channel NALCN. Kschonsak M, Chua HC et al. Nature. 2020 Nov 12;587(7833):313-318.

The 3.2-Å resolution structure of human mTORC2. Scaiola A, Mangia F et al. Sci Adv. 2020 Nov 6;6(45):eabc1251.

Single-particle cryo-EM at atomic resolution. Nakane T, Kotecha A et al. Nature. 2020 Nov 5;587(7832):152-156.

See also: RCSB PDB Images
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News

November 4, 2020

New paper online: UCSF ChimeraX: Structure visualization for researchers, educators, and developers. Pettersen EF, Goddard TD, et al. Protein Sci. 2020, in press.

September 23, 2020

Mac users: ChimeraX v1.1 does not work on MacOS 11.0 (Big Sur), but this problem has been fixed in v1.1.1 and the daily build.

September 10, 2020

The ChimeraX 1.1 production release is available. See the change log for what's new.

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UCSF ChimeraX

UCSF ChimeraX (or simply ChimeraX) is the next-generation molecular visualization program from the Resource for Biocomputing, Visualization, and Informatics (RBVI), following UCSF Chimera. ChimeraX can be downloaded free of charge for academic, government, nonprofit, and personal use. Commercial users, please see ChimeraX commercial licensing.

ChimeraX is developed with support from National Institutes of Health R01-GM129325 and the Office of Cyber Infrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases.

Feature Highlight

membrane protein with lipophilicity coloring

Coloring by Molecular Lipophilicity Potential

Molecular lipophilicity potential (MLP) can be calculated for a protein and displayed with surface coloring using the command mlp or the Molecule Display icon . The image shows the photosynthetic reaction center from a purple sulfur bacterium, with MLP coloring on the molecular surface and membrane boundaries from OPM (Orientations of Proteins in Membranes entry 1eys). Blue and red balls represent the cytoplasmic and periplasmic sides of the bacterial inner membrane, respectively. Parts of the L, M, and H chains span the membrane, whereas the cytochrome subunit sits on the periplasmic side, at the top. The surface coloring ranges from dark goldenrod for the most hydrophobic potentials, through white, to dark cyan for the most hydrophilic. Ligands including lipid, detergent, heme, and various other cofactors are shown as purple surfaces.

For image setup after the structure from OPM has been opened, see the command file mlp.cxc.

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Example Image

neuraminidase flowers

Neuraminidase Flowers

Influenza neuraminidase is an enzyme that promotes the spread of influenza virus among host cells. It is the target of oseltamivir and related antiviral drugs. The image shows tetramers of neuraminidase (PDB 3k3a) styled as flowers. Three tetramers are in different shades of pink, with a central metal ion in white and nearby residues in yellow, and a fourth tetramer is colored green to resemble leaves. Each monomer or “petal” is a six-bladed β-propeller. For image setup other than orientation, see the command file flowers.cxc. The Chimera Image Gallery includes a similar image.

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