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SYXD: Symposium 100 years of X-ray diffraction: from the Laue-experiment to new frontiers

SYXD 1: 100 years of X-ray diffraction: from the Laue experiment to new frontiers (Joint Symposium KR, BP, CPP, DF, MA, MM, GP – Organization: Wiehl, Grübel, Rädler)

SYXD 1.4: Hauptvortrag

Montag, 26. März 2012, 16:30–17:00, H 0105

X-ray free-electron lasers - emerging opportunities for structural biology — •Ilme Schlichting — Max Planck Institute for Medical Research, Heidelberg, Germany

X-ray crystallography is a mature yet still advancing method for structure determination of molecules with any molecular weight. Facilitated greatly by synchrotron X-ray sources, the method is limited only by the quality and size of the crystals and by radiation damage. Free-electron lasers (FELs) provide orders of magnitude brighter and shorter X-ray pulses than conventional synchrotron sources. It has been proposed that radiation damage, which limits the high resolution imaging of soft condensed matter, can be "outrun' by using ultrafast and extremely intense X-ray pulses that pass the sample before the onset of significant radiation damage [1]. Thus, one of the most promising scientific applications of XFELs is in sub-nanometer resolution imaging of biological objects, including viruses, macromolecular assemblies, and nanocrystals. The concept of "diffraction-before-destruction" has been demonstrated recently at the Linac Coherent Light Source (LCLS) [2], the first operational hard X-ray FEL, for protein micro- and nanocrystals [3] and single mimivirus particles [4]. These experiments and recent developments and progress will be presented.

[1]. Neutze et al., Nature 406, 752-757 (2000). [2]. Emma, Nature Photonics 4, 641-647 (2010). [3]. Chapman et al., Nature 470, 73-77 (2011). [4]. Seibert et al., Nature 470, 78-81 (2011).