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Featured Citations

Lectins enhance SARS-CoV-2 infection and influence neutralizing antibodies. Lempp FA, Soriaga LB et al. Nature. 2021 Oct 14;598(7880):342-347.

Reconstitution of an intact clock reveals mechanisms of circadian timekeeping. Chavan AG, Swan JA et al. Science. 2021 Oct 8;374(6564):eabd4453.

Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism. Rao Q, Han L et al. Nat Struct Mol Biol. 2021 Oct;28(10):799-810.

Structure of human cytomegalovirus virion reveals host tRNA binding to capsid-associated tegument protein pp150. Liu YT, Strugatsky D et al. Nat Commun. 2021 Sep 17;12(1):5513.

SEQCROW: A ChimeraX bundle to facilitate quantum chemical applications to complex molecular systems. Schaefer AJ, Ingman VM, Wheeler SE. J Comput Chem. 2021 Sep 15;42(24):1750-1754.

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News

May 28, 2021

The ChimeraX 1.2 production release is available. See the change log for what's new.

December 11, 2020

The RBVI wishes you a safe and happy holiday season! See our 2020 card and the gallery of previous cards back to 1985.

November 4, 2020

New paper online: UCSF ChimeraX: Structure visualization for researchers, educators, and developers. Pettersen EF, Goddard TD, et al. Protein Sci. 2020, in press.

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Upcoming Events

November 9, 2021

SBGrid webinar 3pm PST Nov 9 (noon Nov 10 New Zealand time): Second speaker Tom Goddard (3:30pm) will show using AlphaFold-predicted structures for cryoEM modeling in ChimeraX [register for webinar].


UCSF ChimeraX

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 and the Office of Cyber Infrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases.

Feature Highlight

1g74 per-model clipping

Per-Model Clipping

Front/back (rotatable) clipping can be applied selectively to some models but not others. This is most often used to slice a molecular surface but not the corresponding atomic structure.

For example, the protein in PDB entry 1g74 has an oleic acid residue OLA in an interior pocket. The script in pmc.cxc shows the protein surface, activates front clipping for all models, and then turns it off for just the atomic model, as shown in the figure. The clipping plane can be translated and rotated interactively with the mouse .

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Example Image

HIV-1 protease B-factor coloring

B-factor Coloring

Atomic B-factor values are read from PDB and mmCIF input files and assigned as attributes that can be shown with coloring and used in atom specification. This example shows B-factor variation within a structure of the HIV-1 protease bound to an inhibitor (PDB 4hvp). For complete image setup, including positioning, color key, and label, see the command file bfactor.cxc.

Additional color key examples can be found in tutorials: Coloring by Electrostatic Potential, Coloring by Sequence Conservation

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