English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Femtosecond X-ray protein nanocrystallography

Chapman, H. N., Fromme, P., Barty, A., White, T. A., Kirian, R. A., Aquila, A., et al. (2011). Femtosecond X-ray protein nanocrystallography. Nature, 470(7332), 73-77. doi:10.1038/nature09750.

Item is

Basic

show hide
Genre: Journal Article
Alternative Title : Femtosecond X-ray protein nanocrystallography

Files

show Files
hide Files
:
Nature_470_ 2011_73.pdf (Any fulltext), 2MB
 
File Permalink:
-
Name:
Nature_470_ 2011_73.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
OA-Status:
Locator:
http://dx.doi.org/10.1038/nature09750 (Any fulltext)
Description:
-
OA-Status:

Creators

show
hide
 Creators:
Chapman, Henry N., Author
Fromme, Petra, Author
Barty, Anton, Author
White, Thomas A., Author
Kirian, Richard A., Author
Aquila, Andrew, Author
Hunter, Mark S., Author
Schulz, Joachim, Author
DePonte, Daniel P., Author
Weierstall, Uwe, Author
Doak, R. Bruce1, Author           
Filipe R. N. C. Maia, Filipe R. N. C., Author
Martin, Andrew V., Author
Schlichting, Ilme1, Author           
Lomb, Lukas1, Author           
Coppola, Nicola, Author
Shoeman, Robert L.1, Author           
Epp, Sascha W., Author
Hartmann, Robert, Author
Rolles, Daniel1, Author           
Rudenko, Artem, AuthorFoucar, Lutz1, Author           Kimmel, Nils, AuthorWeidenspointner, Georg, AuthorHoll, Peter, AuthorLiang, Mengning, AuthorBarthelmess, Miriam, AuthorCaleman, Carl, AuthorBoutet, Sébastien, AuthorBogan, Michael J., AuthorKrzywinski, Jacek, AuthorBostedt, Christoph, AuthorBajt, Saša, AuthorGumprecht, Lars, AuthorRudek, Benedikt1, Author           Erk, Benjamin1, Author           Schmidt, Carlo, AuthorHömke, André, AuthorReich, Christian, AuthorPietschner, Daniel, AuthorStrüder, Lothar, AuthorHauser, Günter, AuthorGorke, Hubert, AuthorUllrich, Joachim, AuthorHerrmann, Sven, AuthorSchaller, Gerhard, AuthorSchopper, Florian, AuthorSoltau, Heike, AuthorKühnel, Kai−Uwe, AuthorMesserschmidt, Marc, AuthorBozek, John D., AuthorHau−Riege, Stefan P., AuthorFrank, Matthias, AuthorHampton, Christina Y., AuthorSierra, Raymond G., AuthorStarodub, Dmitri, AuthorWilliams,, Garth J., AuthorHajdu, Janos, AuthorTimneanu, Nicusor, AuthorSeibert, M. Marvin, AuthorAndreasson, Jakob, AuthorRocker, Andrea1, Author           Jönsson, Olof, AuthorSvenda, Martin, AuthorStern, Stephan, AuthorNass, Karol1, Author           Andritschke, Robert, AuthorSchroeter, Claus−Dieter, AuthorKrasniqi, Faton1, Author           Bott, Mario1, Author           Schmidt, Kevin E., AuthorWang, Xiaoyu, AuthorGrotjohann, Ingo, AuthorHolton, James M., AuthorBarends, Thomas1, Author           Neutze, Richard, AuthorMarchesini, Stefano, AuthorFromme, Raimund, AuthorSchorb, Sebastian, AuthorRupp, Daniela, AuthorAdolph, Marcus, AuthorGorkhover, Tais, AuthorAndersson, Inger, AuthorHirsemann, Helmut, AuthorPotdevin, Guillaume, AuthorGraafsma, Heinz, AuthorNilsson, Björn, AuthorSpence, John C. H., Author more..
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

Content

show
hide
Free keywords: -
 Abstract: X-ray crystallography provides the vast majority of macromolecular structures, but the success of the method relies on growing crystals of sufficient size. In conventional measurements, the necessary increase in X-ray dose to record data from crystals that are too small leads to extensive damage before a diffraction signal can be recorded1, 2, 3. It is particularly challenging to obtain large, well-diffracting crystals of membrane proteins, for which fewer than 300 unique structures have been determined despite their importance in all living cells. Here we present a method for structure determination where single-crystal X-ray diffraction ‘snapshots' are collected from a fully hydrated stream of nanocrystals using femtosecond pulses from a hard-X-ray free-electron laser, the Linac Coherent Light Source4. We prove this concept with nanocrystals of photosystem I, one of the largest membrane protein complexes5. More than 3,000,000 diffraction patterns were collected in this study, and a three-dimensional data set was assembled from individual photosystem I nanocrystals (˜200?nm to 2?μm in size). We mitigate the problem of radiation damage in crystallography by using pulses briefer than the timescale of most damage processes6. This offers a new approach to structure determination of macromolecules that do not yield crystals of sufficient size for studies using conventional radiation sources or are particularly sensitive to radiation damage

Details

show
hide
Language(s): eng - English
 Dates: 2010-07-242010-12-092011-02-022011-02-03
 Publication Status: Issued
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 664463
DOI: 10.1038/nature09750
Other: 7738
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nature
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 470 (7332) Sequence Number: - Start / End Page: 73 - 77 Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238