2020
DOI: 10.1038/s41566-020-0607-z
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A MHz-repetition-rate hard X-ray free-electron laser driven by a superconducting linear accelerator

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Cited by 428 publications
(239 citation statements)
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“…The advancing XFELs feature super-conducting accelerator technologies which boost further the brilliance of the current XFEL sources reaching MHz repetition rates. [5][6][7][8] X-ray Photon Correlation Spectroscopy (XPCS) [9][10][11][12][13][14][15][16] is a coherent scattering technique that benefits particularly from this increase in coherent flux holding the potential of capturing structural dynamics at variable length scales, ranging from the nanoscale down to atomic scales. [17][18][19][20] One distinct advantage of XPCS experiments employing the new X-ray sources is the possibility to study dynamics in transient samples (e.g., deeply supercooled water) which are only stable for a short period of time.…”
Section: Introductionmentioning
confidence: 99%
“…The advancing XFELs feature super-conducting accelerator technologies which boost further the brilliance of the current XFEL sources reaching MHz repetition rates. [5][6][7][8] X-ray Photon Correlation Spectroscopy (XPCS) [9][10][11][12][13][14][15][16] is a coherent scattering technique that benefits particularly from this increase in coherent flux holding the potential of capturing structural dynamics at variable length scales, ranging from the nanoscale down to atomic scales. [17][18][19][20] One distinct advantage of XPCS experiments employing the new X-ray sources is the possibility to study dynamics in transient samples (e.g., deeply supercooled water) which are only stable for a short period of time.…”
Section: Introductionmentioning
confidence: 99%
“…X-ray free-electron-lasers (XFELs) are state-of-the-art research instruments that have revolutionized science by enabling the observation of matter at atomic length and time scales [1][2][3][4][5][6][7][8][9][10]. The FEL process is driven by a highbrightness electron beam that travels through an undulator.…”
Section: Introductionmentioning
confidence: 99%
“…The extreme peak brightness and ultrashort pulses provided by X-ray free-electron lasers (XFEL) [1][2][3][4][5] allow data collection from micrometersized protein crystals at room temperature (the functional temperature of their constituent molecules) while outrunning radiation damage. This 'diffraction-before-destruction approach' has been applied in serial femtosecond crystallography (SFX), which has revolutionized X-ray crystallography and has been considered an important tool to determine the structure of proteins that are di cult to crystallize [6][7][8][9] .…”
Section: Introductionmentioning
confidence: 99%