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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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).
Molecular lipophilicity potential (MLP) can be calculated for a protein and shown with surface coloring using the command mlp. The outer-membrane protein CymA allows the diffusion of bulky molecules into the periplasmic space of Klebsiella oxytoca. The image shows CymA (PDB 4d5d chain A) with an α-cyclodextrin molecule (purple) bound at the entry site; a β-cyclodextrin molecule (not visible) is bound inside, near the other end of the pore. The surface coloring ranges from dark goldenrod for the most hydrophobic potentials, through white, to dark cyan for the most hydrophilic. This coloring and the binding of detergent molecules (pink) together help to identify the membrane-embedded portion of the protein. For image setup other than orientation, see the command file mlp.cxc.More features...
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.