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Type III-B CRISPR-Cas cascade of proteolytic cleavages. Steens JA, Bravo JPK et al. Science. 2024 Feb 2;383(6682):512-519.

Structures, functions and adaptations of the human LINE-1 ORF2 protein. Baldwin ET, van Eeuwen T et al. Nature. 2024 Feb 1;626(7997):194–206.

Template and target-site recognition by human LINE-1 in retrotransposition. Thawani A, Ariza AJF et al. Nature. 2024 Feb 1;626(7997):186–193.

An extensive disulfide bond network prevents tail contraction in Agrobacterium tumefaciens phage Milano. Sonani RR, Palmer LK et al. Nat Commun. 2024 Jan 26;15(1):756.

2.7 Å cryo-EM structure of human telomerase H/ACA ribonucleoprotein. Ghanim GE, Sekne Z et al. Nat Commun. 2024 Jan 25;15(1):746.

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News

January 22, 2024

ChimeraX 1.7.1 is available, with fixes for a few miscellaneous bugs that were identified after the 1.7 release.

December 19, 2023

The ChimeraX 1.7 production release is available! See the change log for what's new. Future Mac releases will require macOS 11 or higher.

November 6, 2023

The ChimeraX 1.7 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, Chan Zuckerberg Initiative grant EOSS4-0000000439, and the Office of Cyber Infrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases.

Feature Highlight

GPCR conservation coloring tube helices

Coloring by Sequence Conservation

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.

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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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