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Volta phase plate cryo-EM of the small protein complex Prx3

Cryo-EM of large, macromolecular assemblies has seen a significant increase in the numbers of high-resolution structures since the arrival of direct electron detectors. However, sub-nanometre resolution cryo-EM structures are rare compared with crystal structure depositions, particularly for relativ...

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Autores principales: Khoshouei, Maryam, Radjainia, Mazdak, Phillips, Amy J., Gerrard, Juliet A., Mitra, Alok K., Plitzko, Jürgen M., Baumeister, Wolfgang, Danev, Radostin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4738354/
https://www.ncbi.nlm.nih.gov/pubmed/26817416
http://dx.doi.org/10.1038/ncomms10534
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author Khoshouei, Maryam
Radjainia, Mazdak
Phillips, Amy J.
Gerrard, Juliet A.
Mitra, Alok K.
Plitzko, Jürgen M.
Baumeister, Wolfgang
Danev, Radostin
author_facet Khoshouei, Maryam
Radjainia, Mazdak
Phillips, Amy J.
Gerrard, Juliet A.
Mitra, Alok K.
Plitzko, Jürgen M.
Baumeister, Wolfgang
Danev, Radostin
author_sort Khoshouei, Maryam
collection PubMed
description Cryo-EM of large, macromolecular assemblies has seen a significant increase in the numbers of high-resolution structures since the arrival of direct electron detectors. However, sub-nanometre resolution cryo-EM structures are rare compared with crystal structure depositions, particularly for relatively small particles (<400 kDa). Here we demonstrate the benefits of Volta phase plates for single-particle analysis by time-efficient cryo-EM structure determination of 257 kDa human peroxiredoxin-3 dodecamers at 4.4 Å resolution. The Volta phase plate improves the applicability of cryo-EM for small molecules and accelerates structure determination.
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spelling pubmed-47383542016-03-04 Volta phase plate cryo-EM of the small protein complex Prx3 Khoshouei, Maryam Radjainia, Mazdak Phillips, Amy J. Gerrard, Juliet A. Mitra, Alok K. Plitzko, Jürgen M. Baumeister, Wolfgang Danev, Radostin Nat Commun Article Cryo-EM of large, macromolecular assemblies has seen a significant increase in the numbers of high-resolution structures since the arrival of direct electron detectors. However, sub-nanometre resolution cryo-EM structures are rare compared with crystal structure depositions, particularly for relatively small particles (<400 kDa). Here we demonstrate the benefits of Volta phase plates for single-particle analysis by time-efficient cryo-EM structure determination of 257 kDa human peroxiredoxin-3 dodecamers at 4.4 Å resolution. The Volta phase plate improves the applicability of cryo-EM for small molecules and accelerates structure determination. Nature Publishing Group 2016-01-28 /pmc/articles/PMC4738354/ /pubmed/26817416 http://dx.doi.org/10.1038/ncomms10534 Text en Copyright © 2016, Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Khoshouei, Maryam
Radjainia, Mazdak
Phillips, Amy J.
Gerrard, Juliet A.
Mitra, Alok K.
Plitzko, Jürgen M.
Baumeister, Wolfgang
Danev, Radostin
Volta phase plate cryo-EM of the small protein complex Prx3
title Volta phase plate cryo-EM of the small protein complex Prx3
title_full Volta phase plate cryo-EM of the small protein complex Prx3
title_fullStr Volta phase plate cryo-EM of the small protein complex Prx3
title_full_unstemmed Volta phase plate cryo-EM of the small protein complex Prx3
title_short Volta phase plate cryo-EM of the small protein complex Prx3
title_sort volta phase plate cryo-em of the small protein complex prx3
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4738354/
https://www.ncbi.nlm.nih.gov/pubmed/26817416
http://dx.doi.org/10.1038/ncomms10534
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