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A MERS-CoV-like mink coronavirus uses ACE2 as an entry receptor. Wang N, Ji W et al. Nature. 2025 Jun 19;642(8068):739–746.
Cryo-EM reveals structural diversity in prolate-headed mycobacteriophage Mycofy1. Li X, Shao Q et al. J Mol Biol. 2025 Jun 15;437(12):169126.
Conformational cycle and small-molecule inhibition mechanism of a plant ABCB transporter in lipid membranes. Liu Y, Liao M. Sci Adv. 2025 Jun 13;11(24):eadv9721.
Cat1 forms filament networks to degrade NAD+ during the type III CRISPR-Cas antiviral response. Baca CF, Majumder P et al. Science. 2025 Jun 12;388(6752):eadv9045.
Swinging lever mechanism of myosin directly shown by time-resolved cryo-EM. Klebl DP, McMillan SN et al. Nature. 2025 Jun 12;642(8067):519–526.
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March 6, 2025
Chimera production release 1.19 is now available, fixing the ability to fetch structures from the PDB (details...).
December 25, 2024
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October 14, 2024
Planned downtime: The Chimera and ChimeraX websites, web services (Blast Protein, Modeller, ...) and cgl.ucsf.edu e-mail will be unavailable starting Monday, Oct 14 10 AM PDT, continuing throughout the week and potentially the weekend (Oct 14-20).
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UCSF Chimera is a program for the interactive visualization and analysis of molecular structures and related data, including density maps, trajectories, and sequence alignments. It is available free of charge for noncommercial use. Commercial users, please see Chimera commercial licensing.
We encourage Chimera users to try ChimeraX for much better performance with large structures, as well as other major advantages and completely new features in addition to nearly all the capabilities of Chimera (details...).
Chimera is no longer under active development. Chimera development was supported by a grant from the National Institutes of Health (P41-GM103311) that ended in 2018.
Feature Highlight
A surface can be colored radially, that is, by distance from a user-specified point. Additional options include coloring by distance from an axis or a plane. Different coloring schemes can be applied.
(More features...)Gallery Sample
The image shows interactions of the delta-1 loop with the rest of hepatitis C virus RNA-dependent RNA polymerase (Protein Data Bank entry 1quv). Loop residues in contact with the rest of the structure (van der Waals overlap ≥ 0.01 Å) are displayed as sticks; interacting surface atoms are shown as red patches. (More samples...)
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