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

MicroED uses very small three-dimensional protein crystals and electron diffraction for structure determination. An improved data collection protocol for MicroED called “continuous rotation” is presented. Here microcrystals are continuously rotated during data collection yielding improved data, and...

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Detalles Bibliográficos
Autores principales: Nannenga, Brent L., Shi, Dan, Leslie, Andrew G. W., Gonen, Tamir
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2014
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4149488/
https://www.ncbi.nlm.nih.gov/pubmed/25086503
http://dx.doi.org/10.1038/nmeth.3043
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author Nannenga, Brent L.
Shi, Dan
Leslie, Andrew G. W.
Gonen, Tamir
author_facet Nannenga, Brent L.
Shi, Dan
Leslie, Andrew G. W.
Gonen, Tamir
author_sort Nannenga, Brent L.
collection PubMed
description MicroED uses very small three-dimensional protein crystals and electron diffraction for structure determination. An improved data collection protocol for MicroED called “continuous rotation” is presented. Here microcrystals are continuously rotated during data collection yielding improved data, and allowing data processing with MOSFLM resulting in improved resolution for the model protein lysozyme. These improvements pave the way for the implementation and application of MicroED with wide applicability in structural biology.
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spelling pubmed-41494882015-03-01 High-resolution structure determination by continuous rotation data collection in MicroED Nannenga, Brent L. Shi, Dan Leslie, Andrew G. W. Gonen, Tamir Nat Methods Article MicroED uses very small three-dimensional protein crystals and electron diffraction for structure determination. An improved data collection protocol for MicroED called “continuous rotation” is presented. Here microcrystals are continuously rotated during data collection yielding improved data, and allowing data processing with MOSFLM resulting in improved resolution for the model protein lysozyme. These improvements pave the way for the implementation and application of MicroED with wide applicability in structural biology. 2014-08-03 2014-09 /pmc/articles/PMC4149488/ /pubmed/25086503 http://dx.doi.org/10.1038/nmeth.3043 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
Nannenga, Brent L.
Shi, Dan
Leslie, Andrew G. W.
Gonen, Tamir
High-resolution structure determination by continuous rotation data collection in MicroED
title High-resolution structure determination by continuous rotation data collection in MicroED
title_full High-resolution structure determination by continuous rotation data collection in MicroED
title_fullStr High-resolution structure determination by continuous rotation data collection in MicroED
title_full_unstemmed High-resolution structure determination by continuous rotation data collection in MicroED
title_short High-resolution structure determination by continuous rotation data collection in MicroED
title_sort high-resolution structure determination by continuous rotation data collection in microed
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4149488/
https://www.ncbi.nlm.nih.gov/pubmed/25086503
http://dx.doi.org/10.1038/nmeth.3043
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