Structural basis of ribosomal frameshifting during translation of the SARS-CoV-2 RNA genome. Bhatt PR, Scaiola A et al. Science. 2021 Jun 18;372(6548):1306-1313.
Substrate and product complexes reveal mechanisms of Hedgehog acylation by HHAT. Jiang Y, Benz TL, Long SB. Science. 2021 Jun 11;372(6547):1215-1219.
Structural insight into SARS-CoV-2 neutralizing antibodies and modulation of syncytia. Asarnow D, Wang B et al. Cell. 2021 Jun 10;184(12):3192-3204.e16.
Prevalent, protective, and convergent IgG recognition of SARS-CoV-2 non-RBD spike epitopes. Voss WN, Hou YJ et al. Science. 2021 Jun 4;372(6546):1108-1112.
Structural insights into the cross-neutralization of SARS-CoV and SARS-CoV-2 by the human monoclonal antibody 47D11. Fedry J, Hurdiss DL et al. Sci Adv. 2021 Jun 2;7(23):eabf5632.See also: RCSB PDB Images
May 28, 2021
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We're looking for somebody to join the ChimeraX development team! Please see the job posting for details.
December 11, 2020
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.
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 .More features...
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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