Femtosecond X-ray diffraction from two-dimensional protein crystals
| Autor: | Alexander Graf, John C. H. Spence, M. Marvin Seibert, Marc Messerschmidt, Kaiqin Chu, Mark S. Hunter, Sébastien Boutet, Bill Pedrini, Garth J. Williams, W. Henry Benner, Gebhard F. X. Schertler, Stephen M. Lane, T. Pardini, Xiao-Dan Li, Anton Barty, Celestino Padeste, Nadia A. Zatsepin, James E. Evans, Ching-Ju Tsai, Matthias Frank, Brent W. Segelke, Stefan P. Hau-Riege, R.A. Kirian, David B. Carlson, Matthew A. Coleman |
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| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Diffraction
Materials science two-dimensional protein crystal Astrophysics::High Energy Astrophysical Phenomena Physics::Optics femtosecond crystallography 02 engineering and technology Biochemistry law.invention 03 medical and health sciences Optics law Physics::Atomic and Molecular Clusters General Materials Science membrane protein lcsh:Science 030304 developmental biology 0303 health sciences business.industry Resolution (electron density) Bragg's law General Chemistry 021001 nanoscience & nanotechnology Condensed Matter Physics Laser Research Papers Crystallography Femtosecond X-ray crystallography lcsh:Q single layer X-ray diffraction 0210 nano-technology business Protein crystallization Ultrashort pulse |
| Zdroj: | Iucrj IUCrJ, Vol 1, Iss 2, Pp 95-100 (2014) |
| ISSN: | 2052-2525 |
| Popis: | Bragg diffraction achieved from two-dimensional protein crystals using femtosecond X-ray laser snapshots is presented. X-ray diffraction patterns from two-dimensional (2-D) protein crystals obtained using femtosecond X-ray pulses from an X-ray free-electron laser (XFEL) are presented. To date, it has not been possible to acquire transmission X-ray diffraction patterns from individual 2-D protein crystals due to radiation damage. However, the intense and ultrafast pulses generated by an XFEL permit a new method of collecting diffraction data before the sample is destroyed. Utilizing a diffract-before-destroy approach at the Linac Coherent Light Source, Bragg diffraction was acquired to better than 8.5 Å resolution for two different 2-D protein crystal samples each less than 10 nm thick and maintained at room temperature. These proof-of-principle results show promise for structural analysis of both soluble and membrane proteins arranged as 2-D crystals without requiring cryogenic conditions or the formation of three-dimensional crystals. |
| Databáze: | OpenAIRE |
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