1. Making the Most of 3D Electron Diffraction: Best Practices to Handle a New Tool.
- Author
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Truong, Khai-Nghi, Ito, Sho, Wojciechowski, Jakub M., Göb, Christian R., Schürmann, Christian J., Yamano, Akihito, Del Campo, Mark, Okunishi, Eiji, Aoyama, Yoshitaka, Mihira, Tomohiro, Hosogi, Naoki, Benet-Buchholz, Jordi, Escudero-Adán, Eduardo Carmelo, White, Fraser J., Ferrara, Joseph D., and Bücker, Robert
- Subjects
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ELECTRON diffraction , *TREHALOSE , *BEST practices , *SINGLE crystals , *SMALL molecules , *CRYSTAL structure - Abstract
Along with the adoption of three-dimensional electron diffraction (3D ED/MicroED) as a mainstream tool for structure determination from sub-micron single crystals, questions about best practices regarding each step along the workflow, from data collection to structure solutions, arise. In this paper, we discuss three particular aspects of a 3D ED/MicroED experiment which, after hundreds of structures solved in Rigaku's laboratories, we have found to be important to consider carefully. First, for a representative model system of a hydrated compound (trehalose dihydrate), we show that cryo-transfer of the sample into the diffractometer is an effective means to prevent dehydration, while cooling of the sample without cryo-transfer yields a marginal improvement only. Next, we demonstrate for a small (tyrosine) and a large (clarithromycin) organic compound, how a simplified and fast workflow for dynamical diffraction calculations can determine absolute crystal structures with high confidence. Finally, we discuss considerations and trade-offs for choosing an optimal effective crystal-to-detector distance; while a long distance is mandatory for a protein (thaumatin) example, even a small molecule with difficult diffraction behavior (cystine) yields superior results at longer distances than the one used by default. [ABSTRACT FROM AUTHOR]
- Published
- 2023
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