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Serial femtosecond crystallography of G protein-coupled receptors

X-ray crystallography of G protein-coupled receptors and other membrane proteins is hampered by difficulties associated with growing sufficiently large crystals that withstand radiation damage and yield high-resolution data at synchrotron sources. We used an x-ray free-electron laser (XFEL) with ind... Full description

Journal Title: Science (New York N.Y.), 20 December 2013, Vol.342(6165), pp.1521-4
Main Author: Liu, Wei
Other Authors: Wacker, Daniel , Gati, Cornelius , Han, Gye Won , James, Daniel , Wang, Dingjie , Nelson, Garrett , Weierstall, Uwe , Katritch, Vsevolod , Barty, Anton , Zatsepin, Nadia A , Li, Dianfan , Messerschmidt, Marc , Boutet, Sébastien , Williams, Garth J , Koglin, Jason E , Seibert, M Marvin , Wang, Chong , Shah, Syed T A , Basu, Shibom , Fromme, Raimund , Kupitz, Christopher , Rendek, Kimberley N , Grotjohann, Ingo , Fromme, Petra , Kirian, Richard A , Beyerlein, Kenneth R , White, Thomas A , Chapman, Henry N , Caffrey, Martin , Spence, John C H , Stevens, Raymond C , Cherezov, Vadim
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1095-9203 ; PMID: 24357322 Version:1 ; DOI: 10.1126/science.1244142
Link: http://pubmed.gov/24357322
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recordid: medline24357322
title: Serial femtosecond crystallography of G protein-coupled receptors
format: Article
creator:
  • Liu, Wei
  • Wacker, Daniel
  • Gati, Cornelius
  • Han, Gye Won
  • James, Daniel
  • Wang, Dingjie
  • Nelson, Garrett
  • Weierstall, Uwe
  • Katritch, Vsevolod
  • Barty, Anton
  • Zatsepin, Nadia A
  • Li, Dianfan
  • Messerschmidt, Marc
  • Boutet, Sébastien
  • Williams, Garth J
  • Koglin, Jason E
  • Seibert, M Marvin
  • Wang, Chong
  • Shah, Syed T A
  • Basu, Shibom
  • Fromme, Raimund
  • Kupitz, Christopher
  • Rendek, Kimberley N
  • Grotjohann, Ingo
  • Fromme, Petra
  • Kirian, Richard A
  • Beyerlein, Kenneth R
  • White, Thomas A
  • Chapman, Henry N
  • Caffrey, Martin
  • Spence, John C H
  • Stevens, Raymond C
  • Cherezov, Vadim
subjects:
  • Crystallography, X-Ray -- Instrumentation
  • Receptors, G-Protein-Coupled -- Chemistry
ispartof: Science (New York, N.Y.), 20 December 2013, Vol.342(6165), pp.1521-4
description: X-ray crystallography of G protein-coupled receptors and other membrane proteins is hampered by difficulties associated with growing sufficiently large crystals that withstand radiation damage and yield high-resolution data at synchrotron sources. We used an x-ray free-electron laser (XFEL) with individual 50-femtosecond-duration x-ray pulses to minimize radiation damage and obtained a high-resolution room-temperature structure of a human serotonin receptor using sub-10-micrometer microcrystals grown in a membrane mimetic matrix known as lipidic cubic phase. Compared with the structure solved by using traditional microcrystallography from cryo-cooled crystals of about two orders of magnitude larger volume, the room-temperature XFEL structure displays a distinct distribution of thermal motions and conformations of residues that likely more accurately represent the receptor structure and dynamics in a cellular environment.
language: eng
source:
identifier: E-ISSN: 1095-9203 ; PMID: 24357322 Version:1 ; DOI: 10.1126/science.1244142
fulltext: fulltext
issn:
  • 10959203
  • 1095-9203
url: Link


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titleSerial femtosecond crystallography of G protein-coupled receptors
creatorLiu, Wei ; Wacker, Daniel ; Gati, Cornelius ; Han, Gye Won ; James, Daniel ; Wang, Dingjie ; Nelson, Garrett ; Weierstall, Uwe ; Katritch, Vsevolod ; Barty, Anton ; Zatsepin, Nadia A ; Li, Dianfan ; Messerschmidt, Marc ; Boutet, Sébastien ; Williams, Garth J ; Koglin, Jason E ; Seibert, M Marvin ; Wang, Chong ; Shah, Syed T A ; Basu, Shibom ; Fromme, Raimund ; Kupitz, Christopher ; Rendek, Kimberley N ; Grotjohann, Ingo ; Fromme, Petra ; Kirian, Richard A ; Beyerlein, Kenneth R ; White, Thomas A ; Chapman, Henry N ; Caffrey, Martin ; Spence, John C H ; Stevens, Raymond C ; Cherezov, Vadim
ispartofScience (New York, N.Y.), 20 December 2013, Vol.342(6165), pp.1521-4
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descriptionX-ray crystallography of G protein-coupled receptors and other membrane proteins is hampered by difficulties associated with growing sufficiently large crystals that withstand radiation damage and yield high-resolution data at synchrotron sources. We used an x-ray free-electron laser (XFEL) with individual 50-femtosecond-duration x-ray pulses to minimize radiation damage and obtained a high-resolution room-temperature structure of a human serotonin receptor using sub-10-micrometer microcrystals grown in a membrane mimetic matrix known as lipidic cubic phase. Compared with the structure solved by using traditional microcrystallography from cryo-cooled crystals of about two orders of magnitude larger volume, the room-temperature XFEL structure displays a distinct distribution of thermal motions and conformations of residues that likely more accurately represent the receptor structure and dynamics in a cellular environment.
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titleSerial femtosecond crystallography of G protein-coupled receptors
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atitleSerial femtosecond crystallography of G protein-coupled receptors
jtitleScience (New York, N.Y.)
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abstractX-ray crystallography of G protein-coupled receptors and other membrane proteins is hampered by difficulties associated with growing sufficiently large crystals that withstand radiation damage and yield high-resolution data at synchrotron sources. We used an x-ray free-electron laser (XFEL) with individual 50-femtosecond-duration x-ray pulses to minimize radiation damage and obtained a high-resolution room-temperature structure of a human serotonin receptor using sub-10-micrometer microcrystals grown in a membrane mimetic matrix known as lipidic cubic phase. Compared with the structure solved by using traditional microcrystallography from cryo-cooled crystals of about two orders of magnitude larger volume, the room-temperature XFEL structure displays a distinct distribution of thermal motions and conformations of residues that likely more accurately represent the receptor structure and dynamics in a cellular environment.
doi10.1126/science.1244142
pmid24357322
issn00368075
oafree_for_read
date2013-12-20