Discerning best practices in XFEL-based biological crystallography – standards for nonstandard experiments
| Autor: | Alexander Gorel, Ilme Schlichting, Thomas R. M. Barends |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: | |
| Zdroj: | IUCrJ, Vol 8, Iss 4, Pp 532-543 (2021) |
| Druh dokumentu: | article |
| ISSN: | 2052-2525 20522525 |
| DOI: | 10.1107/S205225252100467X |
| Popis: | Serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs) is a novel tool in structural biology. In contrast to conventional crystallography, SFX relies on merging partial intensities acquired with X-ray beams of often randomly fluctuating properties from a very large number of still diffraction images of generally randomly oriented microcrystals. For this reason, and possibly due to limitations of the still evolving data-analysis programs, XFEL-derived SFX data are typically of a lower quality than `standard' crystallographic data. In contrast with this, the studies performed at XFELs often aim to investigate issues that require precise high-resolution data, for example to determine structures of intermediates at low occupancy, which often display very small conformational changes. This is a potentially dangerous combination and underscores the need for a critical evaluation of procedures including data-quality standards in XFEL-based structural biology. Here, such concerns are addressed. |
| Databáze: | Directory of Open Access Journals |
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