Abstract
Serial femtosecond crystallography is an X-ray free-electron-laser-based method with considerable potential to have an impact on challenging problems in structural biology. Here we present X-ray diffraction data recorded from microcrystals of the Blastochloris viridis photosynthetic reaction centre to 2.8 Å resolution and determine its serial femtosecond crystallography structure to 3.5 Å resolution. Although every microcrystal is exposed to a dose of 33 MGy, no signs of X-ray-induced radiation damage are visible in this integral membrane protein structure.
| Original language | English (US) |
|---|---|
| Article number | 2911 |
| Journal | Nature Communications |
| Volume | 4 |
| DOIs | |
| State | Published - Dec 19 2013 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Chemistry(all)
- Biochemistry, Genetics and Molecular Biology(all)
- Physics and Astronomy(all)
Cite this
Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography. / Johansson, Linda C.; Arnlund, David; Katona, Gergely; White, Thomas A.; Barty, Anton; Deponte, Daniel P.; Shoeman, Robert L.; Wickstrand, Cecilia; Sharma, Amit; Williams, Garth J.; Aquila, Andrew; Bogan, Michael J.; Caleman, Carl; Davidsson, Jan; Doak, R. Bruce; Frank, Matthias; Fromme, Raimund; Galli, Lorenzo; Grotjohann, Ingo; Hunter, Mark S.; Kassemeyer, Stephan; Kirian, Richard A.; Kupitz, Christopher; Liang, Mengning; Lomb, Lukas; Malmerberg, Erik; Martin, Andrew V.; Messerschmidt, Marc; Nass, Karol; Redecke, Lars; Seibert, M. Marvin; Sjöhamn, Jennie; Steinbrener, Jan; Stellato, Francesco; Wang, Dingjie; Wahlgren, Weixaio Y.; Weierstall, Uwe; Westenhoff, Sebastian; Zatsepin, Nadia A.; Boutet, Sébastien; Spence, John C.H.; Schlichting, Ilme; Chapman, Henry N.; Fromme, Petra; Neutze, Richard.
In: Nature Communications, Vol. 4, 2911, 19.12.2013.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography
AU - Johansson, Linda C.
AU - Arnlund, David
AU - Katona, Gergely
AU - White, Thomas A.
AU - Barty, Anton
AU - Deponte, Daniel P.
AU - Shoeman, Robert L.
AU - Wickstrand, Cecilia
AU - Sharma, Amit
AU - Williams, Garth J.
AU - Aquila, Andrew
AU - Bogan, Michael J.
AU - Caleman, Carl
AU - Davidsson, Jan
AU - Doak, R. Bruce
AU - Frank, Matthias
AU - Fromme, Raimund
AU - Galli, Lorenzo
AU - Grotjohann, Ingo
AU - Hunter, Mark S.
AU - Kassemeyer, Stephan
AU - Kirian, Richard A.
AU - Kupitz, Christopher
AU - Liang, Mengning
AU - Lomb, Lukas
AU - Malmerberg, Erik
AU - Martin, Andrew V.
AU - Messerschmidt, Marc
AU - Nass, Karol
AU - Redecke, Lars
AU - Seibert, M. Marvin
AU - Sjöhamn, Jennie
AU - Steinbrener, Jan
AU - Stellato, Francesco
AU - Wang, Dingjie
AU - Wahlgren, Weixaio Y.
AU - Weierstall, Uwe
AU - Westenhoff, Sebastian
AU - Zatsepin, Nadia A.
AU - Boutet, Sébastien
AU - Spence, John C.H.
AU - Schlichting, Ilme
AU - Chapman, Henry N.
AU - Fromme, Petra
AU - Neutze, Richard
PY - 2013/12/19
Y1 - 2013/12/19
N2 - Serial femtosecond crystallography is an X-ray free-electron-laser-based method with considerable potential to have an impact on challenging problems in structural biology. Here we present X-ray diffraction data recorded from microcrystals of the Blastochloris viridis photosynthetic reaction centre to 2.8 Å resolution and determine its serial femtosecond crystallography structure to 3.5 Å resolution. Although every microcrystal is exposed to a dose of 33 MGy, no signs of X-ray-induced radiation damage are visible in this integral membrane protein structure.
AB - Serial femtosecond crystallography is an X-ray free-electron-laser-based method with considerable potential to have an impact on challenging problems in structural biology. Here we present X-ray diffraction data recorded from microcrystals of the Blastochloris viridis photosynthetic reaction centre to 2.8 Å resolution and determine its serial femtosecond crystallography structure to 3.5 Å resolution. Although every microcrystal is exposed to a dose of 33 MGy, no signs of X-ray-induced radiation damage are visible in this integral membrane protein structure.
UR - http://www.scopus.com/inward/record.url?scp=84890950819&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84890950819&partnerID=8YFLogxK
U2 - 10.1038/ncomms3911
DO - 10.1038/ncomms3911
M3 - Article
C2 - 24352554
AN - SCOPUS:84890950819
VL - 4
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
M1 - 2911
ER -