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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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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:
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
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author 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
author_facet 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
author_sort de la Cruz, M. Jason
collection PubMed
description 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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spelling pubmed-53762362017-08-13 Atomic resolution structures from fragmented protein crystals by the cryoEM method MicroED 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 Nat Methods Article 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. 2017-02-13 /pmc/articles/PMC5376236/ /pubmed/28192420 http://dx.doi.org/10.1038/nmeth.4178 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
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
Atomic resolution structures from fragmented protein crystals by the cryoEM method MicroED
title Atomic resolution structures from fragmented protein crystals by the cryoEM method MicroED
title_full Atomic resolution structures from fragmented protein crystals by the cryoEM method MicroED
title_fullStr Atomic resolution structures from fragmented protein crystals by the cryoEM method MicroED
title_full_unstemmed Atomic resolution structures from fragmented protein crystals by the cryoEM method MicroED
title_short Atomic resolution structures from fragmented protein crystals by the cryoEM method MicroED
title_sort atomic resolution structures from fragmented protein crystals by the cryoem method microed
topic Article
url 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
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