High-resolution structure determination by continuous-rotation data collection in MicroEDED

Brent L. Nannenga; Dan Shi; Andrew G.W. Leslie; Tamir Gonen

doi:10.1038/nmeth.3043

High-resolution structure determination by continuous-rotation data collection in MicroEDED

Brent L. Nannenga, Dan Shi, Andrew G.W. Leslie, Tamir Gonen

Research output: Contribution to journal › Article › peer-review

261 Scopus citations

Abstract

MicroEDED uses very small three-dimensional protein crystals and electron diffraction for structure determination. We present an improved data collection protocol for MicroEDED called 'continuous rotation'. Microcrystals are continuously rotated during data collection, yielding more accurate data. The method enables data processing with the crystallographic software tool MOSFMOSFMOSFMOSFLM, which resulted in improved resolution for the model protein lysozyme. These improvements are paving the way for the broad implementation and application of MicroEDED in structural biology.

Original language	English (US)
Pages (from-to)	927-930
Number of pages	4
Journal	Nature Methods
Volume	11
Issue number	9
DOIs	https://doi.org/10.1038/nmeth.3043
State	Published - 2014
Externally published	Yes

ASJC Scopus subject areas

Biotechnology
Biochemistry
Molecular Biology
Cell Biology

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10.1038/nmeth.3043

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title = "High-resolution structure determination by continuous-rotation data collection in MicroEDED",

abstract = "MicroEDED uses very small three-dimensional protein crystals and electron diffraction for structure determination. We present an improved data collection protocol for MicroEDED called 'continuous rotation'. Microcrystals are continuously rotated during data collection, yielding more accurate data. The method enables data processing with the crystallographic software tool MOSFMOSFMOSFMOSFLM, which resulted in improved resolution for the model protein lysozyme. These improvements are paving the way for the broad implementation and application of MicroEDED in structural biology.",

author = "Nannenga, {Brent L.} and Dan Shi and Leslie, {Andrew G.W.} and Tamir Gonen",

note = "Funding Information: The authors thank J. Hattne, F.E. Reyes, D. Olbris, H. Tietz and M. Stumpf for helpful discussions. Work in the Gonen lab is supported by the Howard Hughes Medical Institute. A.G.W.L. is supported by the Medical Research Council (U105184325) and Biotechnology and Biological Sciences Research Council (BBSRC; BB/F020384/1) and Collaborative Computational Project Number 4 (CCP4).",

year = "2014",

doi = "10.1038/nmeth.3043",

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journal = "Nature Methods",

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T1 - High-resolution structure determination by continuous-rotation data collection in MicroEDED

AU - Nannenga, Brent L.

AU - Shi, Dan

AU - Leslie, Andrew G.W.

AU - Gonen, Tamir

N1 - Funding Information: The authors thank J. Hattne, F.E. Reyes, D. Olbris, H. Tietz and M. Stumpf for helpful discussions. Work in the Gonen lab is supported by the Howard Hughes Medical Institute. A.G.W.L. is supported by the Medical Research Council (U105184325) and Biotechnology and Biological Sciences Research Council (BBSRC; BB/F020384/1) and Collaborative Computational Project Number 4 (CCP4).

PY - 2014

Y1 - 2014

N2 - MicroEDED uses very small three-dimensional protein crystals and electron diffraction for structure determination. We present an improved data collection protocol for MicroEDED called 'continuous rotation'. Microcrystals are continuously rotated during data collection, yielding more accurate data. The method enables data processing with the crystallographic software tool MOSFMOSFMOSFMOSFLM, which resulted in improved resolution for the model protein lysozyme. These improvements are paving the way for the broad implementation and application of MicroEDED in structural biology.

AB - MicroEDED uses very small three-dimensional protein crystals and electron diffraction for structure determination. We present an improved data collection protocol for MicroEDED called 'continuous rotation'. Microcrystals are continuously rotated during data collection, yielding more accurate data. The method enables data processing with the crystallographic software tool MOSFMOSFMOSFMOSFLM, which resulted in improved resolution for the model protein lysozyme. These improvements are paving the way for the broad implementation and application of MicroEDED in structural biology.

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High-resolution structure determination by continuous-rotation data collection in MicroEDED

Abstract

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