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Updated: Jun 23, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Powder NMR crystallography of thymol
Elodie Salager1, Robin S Stein, Chris J Pickard
1Université de Lyon, (CNRS/ENS-Lyon/UCB Lyon 1), Centre de RMN à Très Hauts Champs, 5 rue de la Doua, 69100, Villeurbanne, France.
Abstract:
A protocol for the structure determination of powdered solids at natural abundance by NMR is presented and illustrated for the case of the small drug molecule thymol. The procedure uses proton spin-diffusion data from two-dimensional NMR experiments in combination with periodic DFT refinements incorporating (1)H and (13)C NMR chemical shifts. For thymol, the method yields a crystal structure for the powdered sample, which differs by an atomic root-mean-square-deviation (all atoms except methyl group protons) of only 0.07 A from the single crystal X-ray diffraction structure with DFT-optimized proton positions.
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