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Featured Citations

Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion. Walls AC, Tortorici MA et al. Proc Natl Acad Sci USA. 2017 Oct 17;114(42):11157-11162.

Convolutional neural networks for automated annotation of cellular cryo-electron tomograms. Chen M, Dai W et al. Nat Methods. 2017 Oct;14(10):983-985.

Actin-based protrusions of migrating neutrophils are intrinsically lamellar and facilitate direction changes. Fritz-Laylin LK, Riel-Mehan M et al. eLife. 2017 Sep 26;6. pii: e26990.

PDB-Dev: A prototype system for depositing integrative/hybrid structural models. Burley SK, Kurisu G et al. Structure. 2017 Sep 5;25(9):1317-1318.

Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase. Verba KA, Wang RY et al. Science. 2016 Jun 24;352(6293):1542-7.

See also: RCSB PDB Images
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News

November 9, 2017

A fourth alpha release is available. See the change log for salient changes and when they occurred.

October 3, 2017

A third alpha release is available. See the change log for salient changes and when they occurred.

August 15, 2017

A second alpha release is available. To help users decide when to update, we have created a change log listing some of the more significant changes and when they occurred.

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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 licensing.

ChimeraX development is funded by the National Institutes of Health (NIGMS P41-GM103311).

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. 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, see the command file mlp.cxc.

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Example Image

transducin switch regions

G-Protein Switch Regions

The GDP- and GTP-bound conformations of the transducin α-subunit (1tag and 1tnd, respectively) differ primarily in three regions, termed switch 1, switch 2, and switch 3. The structures have been superimposed with matchmaker and shown as cartoons, with “empty” outlines where the structures are almost the same (for simplicity, only one conformation's outlines are shown). The GTP analog GTPγS is displayed as spheres color-coded by heteroatom. For 2D labels and image setup other than structure orientation, see the command file switch.cxc.

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