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Structure of the human inner kinetochore bound to a centromeric CENP-A nucleosome. Yatskevich S, Muir KW et al. Science. 2022 May 20;376(6595):844-852.

The tethered peptide activation mechanism of adhesion GPCRs. Barros-Álvarez X, Nwokonko RM et al. Nature. 2022 Apr 28;604(7907):757–762.

Structural basis for the tethered peptide activation of adhesion GPCRs. Ping YQ, Xiao P et al. Nature. 2022 Apr 28;604(7907):763–770.

Structure of ATP synthase under strain during catalysis. Guo H, Rubinstein JL. Nat Commun. 2022 Apr 25;13(1):2232.

Mechanism of RNA polymerase I selection by transcription factor UAF. Baudin F, Murciano B et al. Sci Adv. 2022 Apr 22;8(16):eabn5725.

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December 20, 2021

The RBVI wishes you a safe and happy holiday season! See our 2021 card and the gallery of previous cards back to 1985.

December 8, 2021

The ChimeraX 1.3 production release is available. See the change log for what's new.

October 22, 2021

The ChimeraX 1.3 release candidate is available. Please try it and report any issues. See the change log for what's new.

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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

CaM-CaMKI peptide

Calmodulin and Target Peptide

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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