Structural basis for strand transfer inhibitor binding to HIV intasomes. Passos DO, Li M et al. Science. 2020 Feb 14;367(6479):810-814.
Structure of an active human histone pre-mRNA 3'-end processing machinery. Sun Y, Zhang Y et al. Science. 2020 Feb 7;367(6478):700-703.
Volatile and thermally stable polymeric tin trifluoroacetates. Bačić G, Rankine CD et al. Inorg Chem. 2020 Jan 21;59(2):996-1005.
Direct visualization of degradation microcompartments at the ER membrane. Albert S, Wietrzynski W et al. Proc Natl Acad Sci USA. 2020 Jan 14;117(2):1069-1080.
Structural basis of substrate recognition by a polypeptide processing and secretion transporter. Kieuvongngam V, Olinares PDB et al. eLife. 2020 Jan 14;9. pii: e51492.(Previously featured citations...)
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UCSF Chimera is a highly extensible program for interactive visualization and analysis of molecular structures and related data, including density maps, supramolecular assemblies, sequence alignments, docking results, trajectories, and conformational ensembles. High-quality images and animations can be generated. Chimera includes complete documentation and several tutorials, and can be downloaded free of charge for academic, government, nonprofit, and personal use. Chimera is developed by the Resource for Biocomputing, Visualization, and Informatics (RBVI), supported in part by the National Institutes of Health (P41-GM103311).
UCSF ChimeraX (or simply ChimeraX) is the next-generation molecular visualization program from the RBVI, following UCSF Chimera.
Protein backbone angles can be shown in a Ramachandran Plot along with probability contours (green lines) from a reference set of well-determined structures. Each amino acid residue is shown as a dot in a graph of φ vs. ψ, more commonly known as a Ramachandran plot or Ramachandran map. Residues are shown as blue dots, or when selected, as red dots. In the example, all helix residues have been selected. Conversely, clicking a dot in the plot will select the corresponding residue in the structure. When the plot has mouse focus, the cursor position (x = φ, y = ψ) is reported under the plot.(More features...)
Side-by-side views of a potassium channel structure (Protein Data Bank entry 1bl8) showing different approaches to cavity detection. On the left are molecular surface patches corresponding to the structure's two largest pockets by MS volume in the Computed Atlas of Surface Topography of proteins (CASTp) database. On the right is a tunnel in blue identified by the MolAxis server. Simple editing converted MolAxis output into a BILD file for display in Chimera. (More samples...)
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