Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED

M. Jason de la Cruz, Johan Hattne, Dan Shi, Paul Seidler, Jose Rodriguez, Francis E. Reyes, Michael R. Sawaya, Duilio Cascio, Simon C. Weiss, Sun Kyung Kim, Cynthia S. Hinck, Andrew P. Hinck, Guillermo Calero, David Eisenberg, Tamir Gonen

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57 Scopus citations

Abstract

Traditionally, crystallographic analysis of macromolecules has depended 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 into microcrystals or nanocrystals can provide a simple path for high-resolution structure determination by the cryoEM method MicroED and potentially by serial femtosecond crystallography.

Original languageEnglish (US)
JournalNature Methods
DOIs
StateAccepted/In press - Feb 13 2017

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ASJC Scopus subject areas

  • Biotechnology
  • Molecular Biology
  • Biochemistry
  • Cell Biology

Cite this

de la Cruz, M. J., Hattne, J., Shi, D., Seidler, P., Rodriguez, J., Reyes, F. E., Sawaya, M. R., Cascio, D., Weiss, S. C., Kim, S. K., Hinck, C. S., Hinck, A. P., Calero, G., Eisenberg, D., & Gonen, T. (Accepted/In press). Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED. Nature Methods. https://doi.org/10.1038/nmeth.4178