Structural Analyses of Bacterial Effectors by X-Ray Crystallography.
| Autor: | Dugelay C; Microbiologie Moléculaire et Biochimie Structurale (MMSB), Université Lyon 1, CNRS, UMR5086, Lyon, France., Gueguen-Chaignon V; Protein Science Facility, SFR Biosciences, Centre National de la Recherche Scientifique UAR3444, Université de Lyon, Lyon, France., Terradot L; Microbiologie Moléculaire et Biochimie Structurale (MMSB), Université Lyon 1, CNRS, UMR5086, Lyon, France. laurent.terradot@ibcp.fr. |
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| Jazyk: | angličtina |
| Zdroj: | Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2024; Vol. 2715, pp. 485-502. |
| DOI: | 10.1007/978-1-0716-3445-5_29 |
| Abstrakt: | X-ray crystallography is a method of choice to determine and analyze protein structures. Although large complexes are challenging to crystallize and cryo-electron microscopy is thus better suited for these, crystallography can still be efficient in solving structures of single components of secretion systems or effectors. Many of the different steps leading to structure determination by X-ray crystallography have been automatized. Here, we describe a generic approach to obtain crystals, solve the structure of a given protein, and perform a preliminary analysis, highlighting novel and efficient possibilities offered by automatization and contribution of Alpha Fold 2 structure prediction. (© 2024. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.) |
| Databáze: | MEDLINE |
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