Description
The advent and application of the X-ray free-electron laser (XFEL) has uncovered the structures of proteins that could not previously be solved using traditional crystallography. While this new technology is powerful, optimization of the process is still needed to improve data quality and analysis efficiency.
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Contributors
- Abdallah, Bahige (Author)
- Zatsepin, Nadia (Author)
- Roy Chowdhury, Shatabdi (Author)
- Coe, Jesse (Author)
- Conrad, Chelsie (Author)
- Dorner, Katerina (Author)
- Sierra, Raymond G. (Author)
- Stevenson, Hilary P. (Author)
- Camacho Alanis, Fernanda (Author)
- Grant, Thomas D. (Author)
- Nelson, Garrett (Author)
- James, Daniel (Author)
- Calero, Guillermo (Author)
- Wachter, Rebekka (Author)
- Spence, John (Author)
- Weierstall, Uwe (Author)
- Fromme, Petra (Author)
- Ros, Alexandra (Author)
- Department of Chemistry and Biochemistry (Contributor)
- College of Liberal Arts and Sciences (Contributor)
- School of Molecular Sciences (Contributor)
- Biodesign Institute (Contributor)
- Applied Structural Discovery (Contributor)
- Department of Physics (Contributor)
Date Created
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2015-08-19
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Identifier
- Digital object identifier: 10.1063/1.4928688
- Identifier TypeInternational standard serial numberIdentifier Value2329-7778
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Abdallah, B. G., Zatsepin, N. A., Roy-Chowdhury, S., Coe, J., Conrad, C. E., Dörner, K., . . . Ros, A. (2015). Microfluidic sorting of protein nanocrystals by size for X-ray free-electron laser diffraction. Structural Dynamics, 2(4), 041719. doi:10.1063/1.4928688