Routine sub-2.5 Å cryo-EM structure determination of GPCRs

There is a need to optimise cryo-EM data acquisition approaches to improve the resolution of GPCR cryo-EM structures to better than 2.5 Å, in order to use them for structure-based drug design purposes. Here, the authors present a systematic analysis of the main cryo-EM experimental parameters using...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Radostin Danev, Matthew Belousoff, Yi-Lynn Liang, Xin Zhang, Fabian Eisenstein, Denise Wootten, Patrick M. Sexton
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/4b98c85f04bd463f9b6c1fcd192b0ef8
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:4b98c85f04bd463f9b6c1fcd192b0ef8
record_format	dspace
spelling	oai:doaj.org-article:4b98c85f04bd463f9b6c1fcd192b0ef82021-12-02T16:08:13ZRoutine sub-2.5 Å cryo-EM structure determination of GPCRs10.1038/s41467-021-24650-32041-1723https://doaj.org/article/4b98c85f04bd463f9b6c1fcd192b0ef82021-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-24650-3https://doaj.org/toc/2041-1723There is a need to optimise cryo-EM data acquisition approaches to improve the resolution of GPCR cryo-EM structures to better than 2.5 Å, in order to use them for structure-based drug design purposes. Here, the authors present a systematic analysis of the main cryo-EM experimental parameters using three GPCRs as test cases, which is also of interest for the cryo-EM structure determination of other small membrane proteins.Radostin DanevMatthew BelousoffYi-Lynn LiangXin ZhangFabian EisensteinDenise WoottenPatrick M. SextonNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Radostin Danev Matthew Belousoff Yi-Lynn Liang Xin Zhang Fabian Eisenstein Denise Wootten Patrick M. Sexton Routine sub-2.5 Å cryo-EM structure determination of GPCRs
description	There is a need to optimise cryo-EM data acquisition approaches to improve the resolution of GPCR cryo-EM structures to better than 2.5 Å, in order to use them for structure-based drug design purposes. Here, the authors present a systematic analysis of the main cryo-EM experimental parameters using three GPCRs as test cases, which is also of interest for the cryo-EM structure determination of other small membrane proteins.
format	article
author	Radostin Danev Matthew Belousoff Yi-Lynn Liang Xin Zhang Fabian Eisenstein Denise Wootten Patrick M. Sexton
author_facet	Radostin Danev Matthew Belousoff Yi-Lynn Liang Xin Zhang Fabian Eisenstein Denise Wootten Patrick M. Sexton
author_sort	Radostin Danev
title	Routine sub-2.5 Å cryo-EM structure determination of GPCRs
title_short	Routine sub-2.5 Å cryo-EM structure determination of GPCRs
title_full	Routine sub-2.5 Å cryo-EM structure determination of GPCRs
title_fullStr	Routine sub-2.5 Å cryo-EM structure determination of GPCRs
title_full_unstemmed	Routine sub-2.5 Å cryo-EM structure determination of GPCRs
title_sort	routine sub-2.5 å cryo-em structure determination of gpcrs
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/4b98c85f04bd463f9b6c1fcd192b0ef8
work_keys_str_mv	AT radostindanev routinesub25acryoemstructuredeterminationofgpcrs AT matthewbelousoff routinesub25acryoemstructuredeterminationofgpcrs AT yilynnliang routinesub25acryoemstructuredeterminationofgpcrs AT xinzhang routinesub25acryoemstructuredeterminationofgpcrs AT fabianeisenstein routinesub25acryoemstructuredeterminationofgpcrs AT denisewootten routinesub25acryoemstructuredeterminationofgpcrs AT patrickmsexton routinesub25acryoemstructuredeterminationofgpcrs
_version_	1718384592379969536

Routine sub-2.5 Å cryo-EM structure determination of GPCRs

Ejemplares similares