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Featured Citations

Structural basis of mammalian respiratory complex I inhibition by medicinal biguanides. Bridges HR, Blaza JN et al. Science. 2023 Jan 27;379(6630):351-357.

Structures of the holo CRISPR RNA-guided transposon integration complex. Park JU, Tsai AW et al. Nature. 2023 Jan 26;613(7945):775-782.

Undecaprenyl phosphate translocases confer conditional microbial fitness. Sit B, Srisuknimit V et al. Nature. 2023 Jan 26;613(7945):721-728.

RNA targeting unleashes indiscriminate nuclease activity of CRISPR-Cas12a2. Bravo JPK, Hallmark T et al. Nature. 2023 Jan 19;613(7944):582–587.

A quantitative map of nuclear pore assembly reveals two distinct mechanisms. Otsuka S, Tempkin JOB et al. Nature. 2023 Jan 19;613(7944):575–581.

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December 21, 2022

The RBVI wishes you a safe and happy holiday season! See our 2022 card and the gallery of previous cards back to 1985.

December 20, 2022

Brought to you by the Brown Lab at Virginia Tech: ChimeraX Tutorial: Making a Holiday Tree!

November 23, 2022

The ChimeraX 1.5 production release is available! 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

heterodimer modeling screenshot

Multichain Comparative Modeling

Modeller Comparative is an interface to Modeller for comparative (“homology”) modeling of proteins and protein complexes.

The example shows modeling the human (shades of blue) from the mouse (brown and tan) complex of programmed death-1 (PD-1) with its ligand PD-L2, PDB 3bp5.

Comparative modeling requires a template structure and a target-template sequence alignment for each unique chain. The sequences of human PD-1 and PD-L2 targets were fetched from UniProt and associated with the corresponding chains in the template structure, see model-pdl-setup.cxc. (Pairwise or multiple sequence alignments could have been used, but in this case, the template structure was simply associated with the target sequence.) Sequence-structure association shows mismatches in the Sequence Viewer: pink boxes for sequence differences between mouse and human, and gray outlines around the parts missing from the structure.

Three models were made with with default settings (other than the number of models), and the best-scoring model is shown. Two positions where sequence differences change the interfacial H-bonds are displayed.

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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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