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04.01.3 Crystallography without Crystals: Breaking the Crystallization Paradigm Dilano Saldin , Hin-Cheuck Poon , Henry Chapman , John Spence

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University of Wisconsin-Milwaukee, Milwaukee, WI, United States, Center for Free Electron 3 Laser Science, Hamburg, Germany, Arizona State University, Tempe, AZ, United States The extreme brilliance of the x-ray free electron laser (XFEL) has provoked speculation about 1 the possibility of protein structure determination from single molecules . However, even in the proposed diffract and destroy experiment, the number of scattered photons per detector pixel 2 from a typical protein is estimated to be a number much less than unity . Methods have been 2,3,4 proposed for structure determination even under such circumstances . We propose a method for structure determination of uncrystallized proteins, by directly recovering the diffraction pattern of a single molecule from that of multiple randomly positioned and randomly oriented ones through their correlated scattering, and subsequent iterative phasing of this 5 diffraction pattern to recover the molecular electron density . We suggest a possible 6 application to structure determinations of membrane proteins in situ . Possible applications for the proposed single-molecule XFEL experiments will also be discussed, as well as ideas for 3,7 extracting time-resolved information . References [1] R. Neutze, et al., Nature 406, 752 (2000). [2] R. Fung et al., Nature Physics 5, 64 (2009). [3] D. K. Saldin et al., J. Phys: Condens. Matter 21, 134014 (2009). [4] N.-T. D. Loh and V. Elser, Phys. Rev. E 80, 026705 (2009). [5] D. K. Saldin et al., New J. Phys., in press [6] D. K. Saldin et al., submitted to Phys. Rev. B. [7] J. C. H. Spence et al., Abstracts of the Meeting of the Microscopical Society of America (2010).



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