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Structure of catalase determined by MicroED

MicroED is a recently developed method that uses electron diffraction for structure determination from very small three-dimensional crystals of biological material. Previously we used a series of still diffraction patterns to determine the structure of lysozyme at 2.9 Å resolution with MicroED (Shi...

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Autores principales: Nannenga, Brent L, Shi, Dan, Hattne, Johan, Reyes, Francis E, Gonen, Tamir
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4359365/
https://www.ncbi.nlm.nih.gov/pubmed/25303172
http://dx.doi.org/10.7554/eLife.03600
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author Nannenga, Brent L
Shi, Dan
Hattne, Johan
Reyes, Francis E
Gonen, Tamir
author_facet Nannenga, Brent L
Shi, Dan
Hattne, Johan
Reyes, Francis E
Gonen, Tamir
author_sort Nannenga, Brent L
collection PubMed
description MicroED is a recently developed method that uses electron diffraction for structure determination from very small three-dimensional crystals of biological material. Previously we used a series of still diffraction patterns to determine the structure of lysozyme at 2.9 Å resolution with MicroED (Shi et al., 2013). Here we present the structure of bovine liver catalase determined from a single crystal at 3.2 Å resolution by MicroED. The data were collected by continuous rotation of the sample under constant exposure and were processed and refined using standard programs for X-ray crystallography. The ability of MicroED to determine the structure of bovine liver catalase, a protein that has long resisted atomic analysis by traditional electron crystallography, demonstrates the potential of this method for structure determination. DOI: http://dx.doi.org/10.7554/eLife.03600.001
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spelling pubmed-43593652015-03-16 Structure of catalase determined by MicroED Nannenga, Brent L Shi, Dan Hattne, Johan Reyes, Francis E Gonen, Tamir eLife Biochemistry MicroED is a recently developed method that uses electron diffraction for structure determination from very small three-dimensional crystals of biological material. Previously we used a series of still diffraction patterns to determine the structure of lysozyme at 2.9 Å resolution with MicroED (Shi et al., 2013). Here we present the structure of bovine liver catalase determined from a single crystal at 3.2 Å resolution by MicroED. The data were collected by continuous rotation of the sample under constant exposure and were processed and refined using standard programs for X-ray crystallography. The ability of MicroED to determine the structure of bovine liver catalase, a protein that has long resisted atomic analysis by traditional electron crystallography, demonstrates the potential of this method for structure determination. DOI: http://dx.doi.org/10.7554/eLife.03600.001 eLife Sciences Publications, Ltd 2014-10-10 /pmc/articles/PMC4359365/ /pubmed/25303172 http://dx.doi.org/10.7554/eLife.03600 Text en © 2014, Nannenga et al http://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited.
spellingShingle Biochemistry
Nannenga, Brent L
Shi, Dan
Hattne, Johan
Reyes, Francis E
Gonen, Tamir
Structure of catalase determined by MicroED
title Structure of catalase determined by MicroED
title_full Structure of catalase determined by MicroED
title_fullStr Structure of catalase determined by MicroED
title_full_unstemmed Structure of catalase determined by MicroED
title_short Structure of catalase determined by MicroED
title_sort structure of catalase determined by microed
topic Biochemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4359365/
https://www.ncbi.nlm.nih.gov/pubmed/25303172
http://dx.doi.org/10.7554/eLife.03600
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