Atomic resolution structures from fragmented protein crystals by the cryoEM method MicroED

Crystallographic analysis of macromolecules depends on large, well-ordered crystals, which often require significant effort to obtain. Even sizable crystals sometimes suffer from pathologies that render them inappropriate for high-resolution structure determination. Here we show that fragmentation o...

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Detalles Bibliográficos
Autores principales: de la Cruz, M. Jason, Hattne, Johan, Shi, Dan, Seidler, Paul, Rodriguez, Jose, Reyes, Francis E., Sawaya, Michael R., Cascio, Duilio, Weiss, Simon C., Kim, Sun Kyung, Hinck, Cynthia S., Hinck, Andrew P., Calero, Guillermo, Eisenberg, David, Gonen, Tamir
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5376236/
https://www.ncbi.nlm.nih.gov/pubmed/28192420
http://dx.doi.org/10.1038/nmeth.4178
Descripción
Sumario:Crystallographic analysis of macromolecules depends on large, well-ordered crystals, which often require significant effort to obtain. Even sizable crystals sometimes suffer from pathologies that render them inappropriate for high-resolution structure determination. Here we show that fragmentation of large, imperfect crystals can provide a simple path for high-resolution structure determination by serial femtosecond crystallography or the cryoEM method MicroED.

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