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The structure of Csk L-SH2 or C122S mutant domain was solved using the molecular replacement method.
We solved the crystal structure of Ac-AChBP in complex with α-CTx LvIA at 3.4 Å resolution, using the molecular replacement method (Table 1).
We crystallized the Ig V domains of hTIM-1 and hTIM-4 and determined the structures at a resolution of 1.3 Å and 2.3 Å, respectively, using the molecular replacement method (See MATERIALS AND METHODS and Table S1).
The complex structure was determined using the molecular replacement method based on the combination of the models of SCARB2 at neutral pH (PDB code: 4TW2) (Dang et al., 2014) and the mouse Fab (PDB code: 5WTG) (Wang et al., 2017).
The crystal structure was solved using the molecular replacement method from synchrotron data (PF, Japan).
The structure was phased using the molecular replacement method with the synaptotagmin-1 C2B domain structure (PDB accession code 1TJM) as a search model.
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The crystal structure of the helicase catalytic core of DrRecQ was solved using the molecular-replacement method and the Phaser program with the coordinates of EcRecQ derived from a search model [ 13].
The crystal structure of the helicase catalytic core of RecQ from D. radiodurans was solved using the molecular-replacement method with the coordinates of EcRecQ from a search model and was refined at a resolution of 2.80 Å.
The structure of the GAP domain of mouse PlexinA3 (PDB ID: 3IG3) was used as the molecular replacement search model using the Phaser module in the Phenix package (Adams et al., 2002; Mccoy et al., 2007).
The program PHASER (McCoy et al., 2007) was used for the molecular replacement search.
The liganded structures were determined by molecular replacement via PHENIX, though in these cases the unliganded LsrF structure was used as the molecular replacement model and reflections for the Rfree set were selected randomly rather than in resolution shells.
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