Structures of human Nav1.7 channel in complex with auxiliary subunits and animal toxins. Shen H, Liu D et al. Science. 2019 Mar 22;363(6433):1303-1308.
Global computational mutagenesis of domain structures associated with inherited eye disease. Ortiz FW, Sergeev YV. Sci Rep. 2019 Mar 6;9(1):3676.
Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides. Chou SZ, Pollard TD. Proc Natl Acad Sci USA. 2019 Mar 5;116(10):4265-4274.
Cryo-EM of retinoschisin branched networks suggests an intercellular adhesive scaffold in the retina. Heymann JB, Vijayasarathy C et al. J Cell Biol. 2019 Mar 4;218(3):1027-1038.
Assessing the predictive power of relative binding free energy calculations for test cases involving displacement of binding site water molecules. Wahl J, Smieško M. J Chem Inf Model. 2019 Feb 25;59(2):754-765.(Previously featured citations...)
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November 17, 2018
October 22, 2018
Mac users: the 1.13.1 release candidate and recent daily builds contain a fix for Mojave (OS 10.14). These versions require OS 10.10 or later.
September 21, 2018
Mac users are advised to hold off upgrading to Mojave until we find a fix for Chimera buttons not being shown until the windows containing them are resized.(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), supported in part by the National Institutes of Health (P41-GM103311).
UCSF ChimeraX (or simply ChimeraX) is the next-generation molecular visualization program from the RBVI, following UCSF Chimera.
Amino acid sidechains adopt different conformational states, or rotamers. Rotamers from the Dunbrack backbone-dependent library or the Richardson "penultimate" library can be viewed, evaluated, and incorporated into structures with the Rotamers tool. A residue can be changed into a different conformation of the same type of amino acid or mutated into a different type. Rotamer torsion angles and library probability values are listed in a dialog, along with (optionally) hydrogen bonds, clashes, and agreement with electron density data. Only rotamers chosen in the list are displayed. When a single rotamer is chosen, it can be incorporated into the structure. The image includes 2D labels.(More features...)
Potassium channel (Protein Data Bank entry 1bl8) on a dark slate blue background with potassium ions shown in firebrick. The channel is comprised of four chains. Each chain has been rainbow-colored from blue at the N-terminus to red at the C-terminus, but only the surface of the channel is shown. The surface has been sliced with a per-model clipping plane. The surface cap color is plum except with opacity set to 0.8. The shininess and brightness have been set to 128 and 8, respectively, and the lights on the scene have been moved from their default positions. The subdivision quality (related to the smoothness of the spherical ions) is 5.0, and the molecular surface was computed with probe radius and vertex density set to 1.0 and 6.0, respectively. (More samples...)
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