Cryo-EM structure of the αvβ8 integrin reveals a mechanism for stabilizing integrin extension. Cormier A, Campbell MG et al. Nat Struct Mol Biol. 2018 Aug;25(8):698-704.
A new HIV-1 Rev structure optimizes interaction with target RNA (RRE) for nuclear export. Watts NR, Eren E et al. J Struct Biol. 2018 Aug;203(2):102-108.
Expanded coverage of the 26S proteasome conformational landscape reveals mechanisms of peptidase gating. Eisele MR, Reed RG et al. Cell Rep. 2018 Jul 31;24(5):1301-1315.e5.
Cryo-EM structures of fungal and metazoan mitochondrial calcium uniporters. Baradaran R, Wang C et al. Nature. 2018 Jul 26;559(7715):580-584.
HIV-1 Nefs are cargo-sensitive AP-1 trimerization switches in tetherin downregulation. Morris KL, Buffalo CZ et al. Cell. 2018 Jul 26;174(3):659-671.e14.(Previously featured citations...)
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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.
Space Navigator is an inexpensive ($60) USB input device from 3Dconnexion for moving and rotating models in 3 dimensions. This animation (8 Mb) shows docking a phage enzyme (PDB 1v0e) into an electron microscopy map (EMDB 1333) using a space navigator and mouse. Works with Windows and Mac Chimera versions (details).(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...)