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The complex structure of durvalumab-scFv/PD-L1 was determined by molecular replacement at a resolution of 2.3 Å (Table S1).
Here, the structure of human recombinant P2 was solved using molecular replacement at 1.85-Å resolution (Table 1, Figure 2A).
In order to exclude that the three methionine mutations for phasing induced folding artefacts, the crystal structure of the native protein was solved by molecular replacement at 2.2 Å resolution (Rwork = 21.7%, Rfree = 26.1%; PDB-ID: 3NM7).
The structure was determined by molecular replacement at 2.9 Å resolution.
Subsequently, a second structure solved by molecular replacement at 2.1 Å resolution showed significant interdomain motions, in addition to highlighting the flexibility of the molecule and the importance of crystallographic packing for the stability of the assembly.
We solved its structure using single-wavelength anomalous dispersion to 5.5 Å to generate models for molecular replacement at 3.2 Å, resulting in the first high-resolution view of a Rev-RRE complex.> -wrap-foot> The Rev dimer-RRE structure depicts essential early steps in the assembly of the larger oligomeric complex.
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(B ) 2Fo − Fc electron density map at 3.2 Å after molecular replacement (contoured at 2.0 σ).
The full-length TtNikM2 (amino acids 1 to 230) structure was solved by molecular replacement method at 3.2 Å resolution.
The structure of the complex MltC· 1 was solved by Molecular Replacement (MR) at 2.45 Å resolution, using the native structure of MltC as initial model.
The crystal structure of the RNase H domain from XMRV RT was solved by the molecular replacement method at a resolution of 2.6 Å.
The apo form of the canine enzyme was solved by molecular replacement and refined at a resolution of 3 Å.
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