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Fe-SP was dissolved in DMSO (dimethyl sulfoxide) for experiments in tissue culture and characterized by HPLC and X-ray crystallography (Table 2) with a high resolution x-ray diffraction system (Bruker SMART diffractometer using SHELXTL-97 software; Bruker AXS Inc., Madison, WI).
The structure of dibenzocinnoline 5a was confirmed using X-ray crystallography (Table 2 and ESI †).
Several SOR structures have been determined by X-ray crystallography (Table 7).
As requested by the reviewers, we have updated the crystallography table, in which the B-factors for the protein and ligand are included.
To explore the structure function relationship, we determined the 3D structure of F G A ΔF L through X-ray crystallography (Table S2, ESI †).
Overall, it is encouraging that the structure of more than half of the human flavoproteins was solved by X-ray crystallography (Table 1).
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Two of them, the monoclinic P21 and C2, were analysed by X-ray crystallography (Supplementary Table II).
Small torsional movements during the catalytic reaction that were revealed by time-lapse crystallography (Supplementary Table 1S) suggest that this was an appropriate approximation.
The crystal structure of YePEPT was solved at 3 Å resolution by X-ray crystallography (Methods and Table 1).
The ability of Protein Tomography to visualize protein structures directly in a cellular environment goes beyond the conventional methods used in biological validation studies such as X-ray crystallography and molecular imaging (Table 1).
Four novel crystal forms were identified (three for PR8 NS1 ED and one for Alb/76 NS1 ED) and solved by x-ray crystallography using molecular replacement (Table 1).
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