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Free keywords:
FREE-ELECTRON LASER; ADENOVIRUS FIBER; FEMTOSECOND CRYSTALLOGRAPHY;
PROTEIN NANOCRYSTALLOGRAPHY; POLYCRYSTALLINE FIBERS; SAMPLE DELIVERY;
FIBROUS PROTEIN; RAY; SEQUENCES; PATTERNSChemistry; Crystallography; Materials Science; serial crystallography; coherent X-ray diffractive imaging (CXDI);
single particles; molecular orientation determination; crystalline
fibrils; amyloid;
Abstract:
Serial diffraction data collected at the Linac Coherent Light Source from crystalline amyloid fibrils delivered in a liquid jet show that the fibrils are well oriented in the jet. At low fibril concentrations, diffraction patterns are recorded from single fibrils; these patterns are weak and contain only a few reflections. Methods are developed for determining the orientation of patterns in reciprocal space and merging them in three dimensions. This allows the individual structure amplitudes to be calculated, thus overcoming the limitations of orientation and cylindrical averaging in conventional fibre diffraction analysis. The advantages of this technique should allow structural studies of fibrous systems in biology that are inaccessible using existing techniques.
