Mechanism of target site selection by type V-K CRISPR-associated transposases. George JT, Acree C et al. Science. 2023 Nov 17;382(6672):eadj8543.
A practical guide to machine-learning scoring for structure-based virtual screening. Tran-Nguyen VK, Junaid M et al. Nat Protoc. 2023 Nov;18(11):3460-3511.
Structure and activation mechanism of the rice Salt Overly Sensitive 1 (SOS1) Na+/H+ antiporter. Zhang XY, Tang LH et al. Nat Plants. 2023 Nov;9(11):1924-1936.
Molecular orbital and topological electron density study of n → π* interactions: amides and thioamides cases. Briceño-Vargas FM, Quesadas-Rojas M et al. RSC Adv. 2023 Oct 26;13(45):31321-31329.
Structures illustrate step-by-step mitochondrial transcription initiation. Goovaerts Q, Shen J et al. Nature. 2023 Oct 26:622(7984):872–879.Previously featured citations...
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October 30-31, 2023
Planned downtime: The Chimera and ChimeraX websites and associated web services will be unavailable Oct 30 8am PDT – Oct 31 11:59pm PDT.
April 19, 2023
April 13, 2023
Chimera production release 1.17 is now available. Updating is required to keep using the tools that run Blast Protein, Modeller, and multiple sequence alignment with Clustal Omega or MUSCLE, as these will soon stop working in older versions. See the release notes for details.Previous news...
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.
Given two or more superimposed structures,
Match→Align creates a corresponding sequence alignment.
The user specifies a distance cutoff for residues allowed to be
in the same column of the output alignment.
In proteins, the distances are measured between α-carbons.
The method is independent of residue types and how the
structures were superimposed.
The figure shows a superposition from MatchMaker of five proteins from the SCOP WD40 superfamily and a corresponding sequence alignment from Match→Align, automatically shown in Multalign Viewer. In the sequence alignment, light green and yellow boxes indicate strands and helices, while the headers RMSD and Conservation show spatial and sequence conservation, respectively.
Potassium channel (Protein Data Bank entry 1bl8) on a dark slate blue background with potassium ions shown in firebrick. The channel is comprised of four chains. Each chain has been rainbow-colored from blue at the N-terminus to red at the C-terminus, but only the surface of the channel is shown. The surface has been sliced with a per-model clipping plane. The surface cap color is plum except with opacity set to 0.8. The shininess and brightness have been set to 128 and 8, respectively, and the lights on the scene have been moved from their default positions. The subdivision quality (related to the smoothness of the spherical ions) is 5.0, and the molecular surface was computed with probe radius and vertex density set to 1.0 and 6.0, respectively. (More samples...)
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