2011
DOI: 10.1038/nphoton.2011.297
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Self-terminating diffraction gates femtosecond X-ray nanocrystallography measurements

Abstract: X-ray free-electron lasers have enabled new approaches to the structural determination of protein crystals that are too small or radiation-sensitive for conventional analysis1. For sufficiently short pulses, diffraction is collected before significant changes occur to the sample, and it has been predicted that pulses as short as 10 fs may be required to acquire atomic-resolution structural information1–4. Here, we describe a mechanism unique to ultrafast, ultra-intense X-ray experiments that allows structural … Show more

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Cited by 307 publications
(227 citation statements)
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“…T he recent development of high peak brightness X-ray freeelectron lasers 1 (XFELs) has enabled breakthroughs in several fields, including warm dense plasmas 2 and the diffractive imaging of biological macromolecules [3][4][5][6] . The interpretation of these experiments is facilitated by comparison with computational models of the X-ray matter interaction, in which the models are exploring previously untested intensity regimes.…”
mentioning
confidence: 99%
“…T he recent development of high peak brightness X-ray freeelectron lasers 1 (XFELs) has enabled breakthroughs in several fields, including warm dense plasmas 2 and the diffractive imaging of biological macromolecules [3][4][5][6] . The interpretation of these experiments is facilitated by comparison with computational models of the X-ray matter interaction, in which the models are exploring previously untested intensity regimes.…”
mentioning
confidence: 99%
“…This method of "diffraction-beforedestruction" allows for a delivered radiation dose (energy/ mass) that is orders of magnitude larger than the tolerable dose using longer duration exposures because the pulse terminates before the onset of significant atomic motion [5], thereby bypassing some of the known limitations of conventional synchrotron-based macromolecular crystallography. Such high intensity snapshot diffraction patterns allow for room-temperature structure determination of radiation-sensitive biological macromolecules from crystals of just a few hundred nanometers in size.…”
Section: Introductionmentioning
confidence: 99%
“…In the early experiments at LCLS 11,13 , the experimenters inferred the X-ray pulse duration to explain their results owing to lack of X-ray diagnostics. In the field of molecular imaging and nanocrystallography, ultrashort and temporally well-defined X-ray pulses are crucial as the radiation damage is expected and observed experimentally 14,15 .…”
mentioning
confidence: 99%