Organizing structural principles of the IL-17 ligand-receptor axis. Wilson SC, Caveney NA et al. Nature. 2022 Sep 15;609(7927):622-629.
Mechanism of AAA+ ATPase-mediated RuvAB-Holliday junction branch migration. Wald J, Fahrenkamp D et al. Nature. 2022 Sep 15;609(7927):630-639.
Membranes under the magnetic lens: A dive into the diverse world of membrane protein structures using cryo-EM. Piper SJ, Johnson RM et al. Chem Rev. 2022 Sep 14;122(17):13989-14017.
R-loop formation and conformational activation mechanisms of Cas9. Pacesa M, Loeff L et al. Nature. 2022 Sep 1;609(7925):191-196.
Molecular architecture of nucleosome remodeling and deacetylase sub-complexes by integrative structure determination. Arvindekar S, Jackman MJ et al. Protein Sci. 2022 Sep;31(9):e4387.More citations...
September 27, 2022
Website downtime: The RBVI website (Chimera, ChimeraX, etc.) and RBVI-hosted web services will be down for maintenance from Tue, Sep 27 9pm PDT, through Wed, possibly extending to Thu, Sep 29 5pm PDT.
June 10, 2022
May 10, 2022Previous news...
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, Chan Zuckerberg Initiative grant EOSS4-0000000439, and the Office of Cyber Infrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases.
Atomic structures, including cartoons and molecular surfaces, can be colored by the conservation in an associated multiple sequence alignment. The figure shows a structure of the β2-adrenergic receptor signaling complex (PDB 3sn6) with receptor cartoon colored blue→white→red from least conserved to most conserved. The β2-adrenergic receptor is a member of the class A G-protein-coupled receptor superfamily. Conservation was calculated from a superfamily alignment from PASS2 using the entropy-based measure from AL2CO (included with ChimeraX courtesy of Pei and Grishin). The sequence alignment and step-by-step instructions for making this image are given in the Coloring by Sequence Conservation tutorial.More features...
Calmodulin (CaM) acts as a calcium sensor. When its four Ca++ sites are fully occupied, it binds and modulates the activity of various downstream proteins, including CaM-dependent protein kinase I (CaMKI). Here, a complex between CaM and its target peptide from CaMKI (PDB 1mxe) is shown with cartoons, a transparent molecular surface, silhouette outlines, and light soft ambient occlusion. (If you prefer a less smudgy/rustic appearance, try using light gentle instead.) For image setup other than positioning, see the command file cam.cxc.
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