Selected article for: "asymmetric unit and electron density"

Author: David N. Frick; Rajdeep S. Virdi; Nemanja Vuksanovic; Narayan Dahal; Nicholas R Silvaggi
Title: Variable Macro X Domain of SARS-CoV-2 Retains the Ability to Bind ADP-ribose
  • Document date: 2020_4_2
  • ID: 02q9y011_9
    Snippet: Structure of the SARS-CoV-2 Macro X Domain-The SARS CoV-2 macro X domain (NSP3 residues 207 to 277) crystallized in space group P212121 with 1 molecule per asymmetric unit. These crystals had a solvent content of 43% and diffracted extremely well. The final resolution limit of the data was set at 0.95 Ã… ( Table 1 ). The quality of the electron density maps is correspondingly excellent (Fig. 4A ). The section of the structure depicted in this ima.....
    Document: Structure of the SARS-CoV-2 Macro X Domain-The SARS CoV-2 macro X domain (NSP3 residues 207 to 277) crystallized in space group P212121 with 1 molecule per asymmetric unit. These crystals had a solvent content of 43% and diffracted extremely well. The final resolution limit of the data was set at 0.95 Ã… ( Table 1 ). The quality of the electron density maps is correspondingly excellent (Fig. 4A ). The section of the structure depicted in this image is located on the surface of the protein and the B-factors of these residues are close to the average B-factor of the protein (7.2 vs 10.2 Ã… 2 ), indicating that this sample accurately represents the overall quality of the maps. The final model contains the entire sequence from V207 to S377 of nsp3, an N-terminal glycine residue that was left from the TEV-protease cleavage, and 374 solvent molecules. The Rcryst and Rfree values of the final model were 0.119 and 0.137, respectively ( Table 1) .

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