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Homochiral and racemic MicroED structures of a peptide repeat from the ice-nucleation protein InaZ

The ice-nucleation protein InaZ from Pseudomonas syringae contains a large number of degenerate repeats that span more than a quarter of its sequence and include the segment GSTSTA. Ab initio structures of this repeat segment, resolved to 1.1 Å by microfocus X-ray crystallography and to 0.9 Å by the...

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Autores principales: Zee, Chih-Te, Glynn, Calina, Gallagher-Jones, Marcus, Miao, Jennifer, Santiago, Carlos G., Cascio, Duilio, Gonen, Tamir, Sawaya, Michael R., Rodriguez, Jose A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6400192/
https://www.ncbi.nlm.nih.gov/pubmed/30867917
http://dx.doi.org/10.1107/S2052252518017621
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author Zee, Chih-Te
Glynn, Calina
Gallagher-Jones, Marcus
Miao, Jennifer
Santiago, Carlos G.
Cascio, Duilio
Gonen, Tamir
Sawaya, Michael R.
Rodriguez, Jose A.
author_facet Zee, Chih-Te
Glynn, Calina
Gallagher-Jones, Marcus
Miao, Jennifer
Santiago, Carlos G.
Cascio, Duilio
Gonen, Tamir
Sawaya, Michael R.
Rodriguez, Jose A.
author_sort Zee, Chih-Te
collection PubMed
description The ice-nucleation protein InaZ from Pseudomonas syringae contains a large number of degenerate repeats that span more than a quarter of its sequence and include the segment GSTSTA. Ab initio structures of this repeat segment, resolved to 1.1 Å by microfocus X-ray crystallography and to 0.9 Å by the cryo-EM method MicroED, were determined from both racemic and homochiral crystals. The benefits of racemic protein crystals for structure determination by MicroED were evaluated and it was confirmed that the phase restriction introduced by crystal centrosymmetry increases the number of successful trials during the ab initio phasing of the electron diffraction data. Both homochiral and racemic GSTSTA form amyloid-like protofibrils with labile, corrugated antiparallel β-sheets that mate face to back. The racemic GSTSTA protofibril represents a new class of amyloid assembly in which all-left-handed sheets mate with their all-right-handed counterparts. This determination of racemic amyloid assemblies by MicroED reveals complex amyloid architectures and illustrates the racemic advantage in macromolecular crystallography, now with submicrometre-sized crystals.
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spelling pubmed-64001922019-03-13 Homochiral and racemic MicroED structures of a peptide repeat from the ice-nucleation protein InaZ Zee, Chih-Te Glynn, Calina Gallagher-Jones, Marcus Miao, Jennifer Santiago, Carlos G. Cascio, Duilio Gonen, Tamir Sawaya, Michael R. Rodriguez, Jose A. IUCrJ Research Papers The ice-nucleation protein InaZ from Pseudomonas syringae contains a large number of degenerate repeats that span more than a quarter of its sequence and include the segment GSTSTA. Ab initio structures of this repeat segment, resolved to 1.1 Å by microfocus X-ray crystallography and to 0.9 Å by the cryo-EM method MicroED, were determined from both racemic and homochiral crystals. The benefits of racemic protein crystals for structure determination by MicroED were evaluated and it was confirmed that the phase restriction introduced by crystal centrosymmetry increases the number of successful trials during the ab initio phasing of the electron diffraction data. Both homochiral and racemic GSTSTA form amyloid-like protofibrils with labile, corrugated antiparallel β-sheets that mate face to back. The racemic GSTSTA protofibril represents a new class of amyloid assembly in which all-left-handed sheets mate with their all-right-handed counterparts. This determination of racemic amyloid assemblies by MicroED reveals complex amyloid architectures and illustrates the racemic advantage in macromolecular crystallography, now with submicrometre-sized crystals. International Union of Crystallography 2019-01-24 /pmc/articles/PMC6400192/ /pubmed/30867917 http://dx.doi.org/10.1107/S2052252518017621 Text en © Chih-Te Zee et al. 2019 http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/4.0/
spellingShingle Research Papers
Zee, Chih-Te
Glynn, Calina
Gallagher-Jones, Marcus
Miao, Jennifer
Santiago, Carlos G.
Cascio, Duilio
Gonen, Tamir
Sawaya, Michael R.
Rodriguez, Jose A.
Homochiral and racemic MicroED structures of a peptide repeat from the ice-nucleation protein InaZ
title Homochiral and racemic MicroED structures of a peptide repeat from the ice-nucleation protein InaZ
title_full Homochiral and racemic MicroED structures of a peptide repeat from the ice-nucleation protein InaZ
title_fullStr Homochiral and racemic MicroED structures of a peptide repeat from the ice-nucleation protein InaZ
title_full_unstemmed Homochiral and racemic MicroED structures of a peptide repeat from the ice-nucleation protein InaZ
title_short Homochiral and racemic MicroED structures of a peptide repeat from the ice-nucleation protein InaZ
title_sort homochiral and racemic microed structures of a peptide repeat from the ice-nucleation protein inaz
topic Research Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6400192/
https://www.ncbi.nlm.nih.gov/pubmed/30867917
http://dx.doi.org/10.1107/S2052252518017621
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