Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED
Abstract
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.
- Authors:
-
[1];
[1];
- Howard Hughes Medical Inst., Ashburn, VA (United States). Janelia Research Campus
- Univ. of California, Los Angeles, CA (United States)
- Univ. of Pittsburgh, PA (United States)
- Publication Date:
- Research Org.:
- Univ. of California, Los Angeles, CA (United States)
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1463137
- Grant/Contract Number:
- FC02-02ER63421
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Nature Methods
- Additional Journal Information:
- Journal Volume: 14; Journal Issue: 4; Journal ID: ISSN 1548-7091
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES
Citation Formats
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, and Gonen, Tamir. Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED. United States: N. p., 2017.
Web. doi: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. United States. 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, and Gonen, Tamir. Mon .
"Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED". United States. https://doi.org/10.1038/nmeth.4178. https://www.osti.gov/servlets/purl/1463137.
@article{osti_1463137,
title = {Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED},
author = {de la Cruz, M. Jason and Hattne, Johan and Shi, Dan and Seidler, Paul and Rodriguez, Jose and Reyes, Francis E. and Sawaya, Michael R. and Cascio, Duilio and Weiss, Simon C. and Kim, Sun Kyung and Hinck, Cynthia S. and Hinck, Andrew P. and Calero, Guillermo and Eisenberg, David and Gonen, Tamir},
abstractNote = {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.},
doi = {10.1038/nmeth.4178},
journal = {Nature Methods},
number = 4,
volume = 14,
place = {United States},
year = {Mon Feb 13 00:00:00 EST 2017},
month = {Mon Feb 13 00:00:00 EST 2017}
}
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