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  De novo protein crystal structure determination from X-ray free-electron laser data

Barends, T. R., Foucar, L., Botha, S., Doak, B., Shoeman, R. L., Nass, K., et al. (2014). De novo protein crystal structure determination from X-ray free-electron laser data. Nature, 505(7482), 244-247. doi:10.1038/nature12773.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-8F74-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-8F75-1
Genre: Journal Article

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Barends, Thomas R.M.1, Author              
Foucar, Lutz1, Author              
Botha, Sabine1, Author              
Doak, Bruce1, Author              
Shoeman, Robert L.1, Author              
Nass, Karol1, Author              
Koglin, Jason E., Author
Williams, Garth J., Author
Boutet, Sébastien, Author
Messerschmidt, Marc, Author
Schlichting, Ilme1, Author              
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, Jahnstrasse 29, 69120 Heidelberg, DE, ou_1497700              

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 Abstract: The determination of protein crystal structures is hampered by the need for macroscopic crystals. X-ray free-electron lasers (FELs) provide extremely intense pulses of femtosecond duration, which allow data collection from nanometre- to micrometre-sized crystals1, 2, 3, 4 in a ‘diffraction-before-destruction’ approach. So far, all protein structure determinations carried out using FELs have been based on previous knowledge of related, known structures1, 2, 3, 4, 5. Here we show that X-ray FEL data can be used for de novo protein structure determination, that is, without previous knowledge about the structure. Using the emerging technique of serial femtosecond crystallography1, 2, 3, 4, 6, we performed single-wavelength anomalous scattering measurements on microcrystals of the well-established model system lysozyme, in complex with a lanthanide compound. Using Monte-Carlo integration6, 7, we obtained high-quality diffraction intensities from which experimental phases could be determined, resulting in an experimental electron density map good enough for automated building of the protein structure. This demonstrates the feasibility of determining novel protein structures using FELs. We anticipate that serial femtosecond crystallography will become an important tool for the structure determination of proteins that are difficult to crystallize, such as membrane proteins1, 2, 8.

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 Dates: 2013-07-232013-10-142013-11-242014-01-09
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/nature12773
Other: 7942
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Title: Nature
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 505 (7482) Sequence Number: - Start / End Page: 244 - 247 Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238