![]() ![]() ![]() including high-intensity multiwavelength anomalous diffraction 20,21 20. Towards phasing using high x-ray intensity” (submitted). The latter brings in high-intensity phasing (HIP) methods, 19 19. or one takes an advantage of the large degree of ionization at high x-ray intensity. To overcome the phase problem for x-ray crystallography with XFELs, one uses conventional phasing technique at intermediate x-ray intensity, 18 18.ĭe novo protein crystal structure determination from x-ray free-electron laser data,” Nature 505, 244 (2014). is the bottleneck to reconstruct molecular structures in serial femtosecond crystallography as much as in conventional x-ray crystallography. To investigate molecular structure and structural dynamics with XFELs, one needs to understand radiation damage dynamics-x-ray multiphoton ionization dynamics and accompanying nuclear dynamics. enable us to take a step forward towards molecular movies. Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein,” Science 346, 1242 (2014). Serial time-resolved crystallography of photosystem II using a femtosecond x-ray laser,” Nature 513, 261 (2014). Taking snapshots of photosynthetic water oxidation using femtosecond x-ray diffraction and spectroscopy,” Nat. Simultaneous femtosecond x-ray spectroscopy and diffraction of photosystem II at room temperature,” Science 340, 491 (2013). Time-resolved protein nanocrystallography using an x-ray free-electron laser,” Opt. Recent advances in time-resolved serial femtosecond crystallography 12–16 12. 11.Ĭrystallography using an x-ray free-electron laser,” Crystallogr. Time-resolved structural studies at synchrotrons and x-ray free electron lasers: Opportunities and challenges,” Curr. 9.Įmerging opportunities in structural biology with x-ray free-electron lasers,” Curr. 8–11 8.įemtosecond nanocrystallography using x-ray lasers for membrane protein structure determination,” Curr. promising a breakthrough in structural biology (see reviews in Refs. Natively inhibited Trypanosoma brucei cathepsin B structure determined by using an x-ray laser,” Science 339, 227 (2013). has started to reveal previously unknown protein structure, 7 7. X-ray crystallography with XFELs, after demonstration of the proof-of-principle, 6 6.įemtosecond diffractive imaging with a soft-x-ray free-electron laser,” Nat. One of the most prominent XFEL applications is imaging of biological macromolecules. Unprecedentedly ultraintense and ultrafast hard x-ray pulses generated from XFELs enable us to measure molecular structures on the atomic scale and to explore the structural dynamics on the femtosecond scale. Lin (įree-electron lasers: New avenues in molecular physics and photochemistry,” Annu. The first atomic and molecular experiments at the linac coherent light source x-ray free electron laser,” in Advances in Atomic, Molecular, and Optical Physics, edited by E. Introduction to the new science with x-ray free electron lasers,” Contemp. opens up a new era in science and technology. The history of x-ray free-electron lasers,” Eur. The advent of x-ray free-electron lasers (XFELs) 1,2 1.
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