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

Research output: Contribution to journalArticle

47 Citations (Scopus)

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

Fingerprint

Crystallography
Nanoparticles
Pathology
Crystals
Microcrystals
Proteins
Macromolecules
Nanocrystals

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., ... 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

Atomic-resolution structures from fragmented protein crystals with 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.

In: Nature Methods, 13.02.2017.

Research output: Contribution to journalArticle

de la Cruz, MJ, Hattne, J, Shi, D, Seidler, P, Rodriguez, J, Reyes, FE, Sawaya, MR, Cascio, D, Weiss, SC, Kim, SK, Hinck, CS, Hinck, AP, Calero, G, Eisenberg, D & Gonen, T 2017, 'Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED', Nature Methods. https://doi.org/10.1038/nmeth.4178
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 with the cryoEM method MicroED. In: Nature Methods. 2017.
@article{7988c7bea4104f2ba5ae58e673dd48e8,
title = "Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED",
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.",
author = "{de la Cruz}, {M. Jason} and Johan Hattne and Dan Shi and Paul Seidler and Jose Rodriguez and Reyes, {Francis E.} and Sawaya, {Michael R.} and Duilio Cascio and Weiss, {Simon C.} and Kim, {Sun Kyung} and Hinck, {Cynthia S.} and Hinck, {Andrew P.} and Guillermo Calero and David Eisenberg and Tamir Gonen",
year = "2017",
month = "2",
day = "13",
doi = "10.1038/nmeth.4178",
language = "English (US)",
journal = "Nature Methods",
issn = "1549-1277",
publisher = "Public Library of Science",

}

TY - JOUR

T1 - Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED

AU - de la Cruz, M. Jason

AU - Hattne, Johan

AU - Shi, Dan

AU - Seidler, Paul

AU - Rodriguez, Jose

AU - Reyes, Francis E.

AU - Sawaya, Michael R.

AU - Cascio, Duilio

AU - Weiss, Simon C.

AU - Kim, Sun Kyung

AU - Hinck, Cynthia S.

AU - Hinck, Andrew P.

AU - Calero, Guillermo

AU - Eisenberg, David

AU - Gonen, Tamir

PY - 2017/2/13

Y1 - 2017/2/13

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85012279008&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85012279008&partnerID=8YFLogxK

U2 - 10.1038/nmeth.4178

DO - 10.1038/nmeth.4178

M3 - Article

C2 - 28192420

AN - SCOPUS:85012279008

JO - Nature Methods

JF - Nature Methods

SN - 1549-1277

ER -