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  Protein crystal structure obtained at 2.9 Å resolution from injecting bacterial cells into an X-ray free-electron laser beam

Sawaya, M. R., Cascio, D., Gingery, M., Rodriguez, J., Goldschmidt, L., Colletier, J.-P., et al. (2014). Protein crystal structure obtained at 2.9 Å resolution from injecting bacterial cells into an X-ray free-electron laser beam. Proceedings of the National Academy of Sciences of the United States of America, 111(35), 12769-12774. doi:10.1073/pnas.1413456111.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-951D-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-951E-B
Genre: Journal Article

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PNAS_111_2014_12769.pdf (Any fulltext), 852KB
 
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 Creators:
Sawaya, Michael R., Author
Cascio, Duilio, Author
Gingery, Mari, Author
Rodriguez, Jose, Author
Goldschmidt, Lukasz, Author
Colletier, Jacques-Philippe, Author
Messerschmidt, Marc M., Author
Boutet, Sébastien, Author
Koglin, Jason E., Author
Williams, Garth J., Author
Brewster, Aaron S., Author
Nass, Karol1, Author              
Hattne, Johan, Author
Botha, Sabine1, Author              
Doak, Bruce1, Author              
Shoeman, Robert L.1, Author              
DePonte, Daniel P., Author
Park, Hyun-Woo, Author
Federici, Brian A., Author
Sauter, Nicholas K., Author
Schlichting, Ilme1, Author              Eisenberg, David S., Author more..
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, escidoc:1497700              

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Free keywords: Cry3A insecticidal toxin; XFEL; serial femtosecond crystallography
 Abstract: It has long been known that toxins produced by Bacillus thuringiensis (Bt) are stored in the bacterial cells in crystalline form. Here we describe the structure determination of the Cry3A toxin found naturally crystallized within Bt cells. When whole Bt cells were streamed into an X-ray free-electron laser beam we found that scattering from other cell components did not obscure diffraction from the crystals. The resolution limits of the best diffraction images collected from cells were the same as from isolated crystals. The integrity of the cells at the moment of diffraction is unclear; however, given the short time (∼ 5 µs) between exiting the injector to intersecting with the X-ray beam, our result is a 2.9-Å-resolution structure of a crystalline protein as it exists in a living cell. The study suggests that authentic in vivo diffraction studies can produce atomic-level structural information.

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Language(s): eng - English
 Dates: 2014-07-232014-08-182014-08-182014-09-02
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
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Affiliations:
Publ. Info: National Academy of Sciences
Pages: - Volume / Issue: 111 (35) Sequence Number: - Start / End Page: 12769 - 12774 Identifier: ISSN: 0027-8424
CoNE: http://pubman.mpdl.mpg.de/cone/journals/resource/954925427230