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KR: Fachgruppe Kristallographie

KR 1: SYXD: 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)

KR 1.5: Hauptvortrag

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

Structure analysis by x-ray diffraction and x-ray imaging: beyond crystals, beyond averages, and beyond modeling — •Tim Salditt — Georg-August-Universität Göttingen, Institut für Röntgenphysik, Friedrich-Hund-Platz 1, 37077 Göttingen

Classical x-ray diffraction has been based on three constraints: (i) averages over macroscopic accumulation time and sample sizes, which are many orders of magnitude larger than the structures to be resolved; (ii) homeogeneous "well ordered" samples which are - if not crystalline - characterized by well-defined correlation functions; (iii) data analysis by fitting to modeled diffraction data. However, many condensed matter problems, in particular in functional materials, soft matter and biomolecular samples, address non-equilibrium states with competing length scales, hierachical structures, and intrinsic dynamics. Progress in x-ray sources and optics has helped to meet these challenges. Conceptually often still close to the Laue experiment, far-field diffraction data can now be collected in controllable field of vies, with highly focused beams reaching the 10 nm range. Biomolecular diffraction signals can be recorded from hierachical structures such as a biological cells. Perhaps most importantly, fully coherent illumination enables data inversion without prohibitive model building. How these advances serve science, will be illustrated by examples in neuro-biophysics. We present experiments addressing different structural levels and bridging length scales, from proteins and lipid assemblies up to a complete organelle such as the synaptic vesicle, from an isolated axon up to an unsliced nerve, from tissue slice to the sensory organ.