Abstract Details
| Potential of Coherent Diffractive Imaging for Protein-Nano-Crystallography at Future XFEL Sources | |
|---|---|
| Abstract ID | W_Coherent-1 |
| Presenter | Franz Pfeiffer |
| Presentation Type | Coherent X-ray - LCLS |
| Full Author List | F. Pfeiffer (1,2) , C. M. Kewish (1) , P. Thibault (1) , O. Bunk (1) |
| Affiliations | (1) Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland (2) Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland |
| Category | Instrumentation/Development |
| Abstract | Macromolecular crystallography using synchrotron (or lab-based) x-ray sources is an extremely powerful method with an enormous impact on structural biology. The protein data bank (PDB) today already contains more than 50,000 entries, and the majority of structures were refined from x-ray crystallography data.
Today, in favorable conditions and at state-of-the-art instruments, structures can be solved from protein crystals of a few microns in size [1,2]. However, sample damage ultimately limits the applicability of synchrotron-based macromolecular crystallography for smaller, sub-micron crystals or non-crystalline assemblies. X-ray free-electron lasers (XFELs) are expected to overcome this limitation by circumventing the radiation damage problem using an ultra-fast, femtosecond coherent diffractive imaging (CDI) imaging approach [3,4]. Although it has been speculated that CDI methods in combination with advanced data processing algorithms [5,6] could ultimately be used to solve the structure of a single macromolecule, the initial experiments at future XFELs will probably focus on more straightforward adaptations of macromolecular crystallography concepts. With this contribution we will present one possible scheme of how CDI can be implemented for protein crystallography with two- or three-dimensional nano-crystals at future XFEL sources. We will particularly present numerical results that support the feasibility of using XFELs for structure determination of submicron, two-dimensional membrane protein crystals. |
| Footnotes | [1] F. Coulibaly et al., Nature 446, 97 (2007).
[2] R. Moukhametzianov et al., Acta Cryst. D64, 158 (2008). [3] R. Neutze et al., Nature 406, 753 (2000). [4] H. Chapman et al., Nature Physics 2, 839 (2006). [5] V.L. Shneerson et al., Acta Cryst. A64, 303 (2008). [6] V. Elser, Acta Cryst. A64, 273 (2008). |
| Funding Acknowledgement | |