Abstract
Multiplexing of the Linac Coherent Light Source beam was demonstrated for hard X-rays by spectral division using a near-perfect diamond thin-crystal monochromator operating in the Bragg geometry. The wavefront and coherence properties of both the reflected and transmitted beams were well preserved, thus allowing simultaneous measurements at two separate instruments. In this report, the structure determination of a prototypical protein was performed using serial femtosecond crystallography simultaneously with a femtosecond time-resolved XANES studies of photoexcited spin transition dynamics in an iron spin-crossover system. The results of both experiments using the multiplexed beams are similar to those obtained separately, using a dedicated beam, with no significant differences in quality.
Highlights
The advent of X-ray free-electron lasers (FELs) such as the Linac Coherent Light Source (LCLS) (Emma et al, 2010) in the USA and the SPring-8 Angstrom Compact Free Electron Laser (SACLA) (Ishikawa et al, 2012) in Japan has generated tremendous excitement among the X-ray user community because of the enormous potential of such sources for transforming scientific research in a wide range of disciplines, including physics, chemistry, biology, material science and energy research
The monochromator crystal used was a 105 mm-thick type IIa diamond single-crystal working in the Bragg geometry, producing two well separate beams: one Bragg reflected and monochromatic, the other in transmission with a spectral notch created by the Bragg reflection
In this article we present the findings from performing simultaneous measurements on two benchmarking systems, i.e. serial femtosecond crystallography of the prototypical protein lyzozyme using the transmitted beam; and photoexcited spin transition dynamics studies of an iron spincrossover system, iron(II) tris(2,20-bipyridine) in water via femtosecond time-resolved X-ray Absorption Near-Edge Spectroscopy (XANES) measurement using the Braggreflected beam
Summary
The advent of X-ray free-electron lasers (FELs) such as the Linac Coherent Light Source (LCLS) (Emma et al, 2010) in the USA and the SPring-8 Angstrom Compact Free Electron Laser (SACLA) (Ishikawa et al, 2012) in Japan has generated tremendous excitement among the X-ray user community because of the enormous potential of such sources for transforming scientific research in a wide range of disciplines, including physics, chemistry, biology, material science and energy research. The demand for user access has steadily increased, leading to approximately only one out of five user proposals being granted beam time at LCLS. This shortfall stems from the serial nature of X-ray FEL operation whereby a single undulator (Emma et al, 2010) typically can only provide the beam to one experimental station at any given time, in strong contrast to the scenario at storage-ring synchrotron X-ray sources where many tens of instruments can receive X-ray beams concurrently. In this article we present the findings from performing simultaneous measurements on two benchmarking systems, i.e. serial femtosecond crystallography of the prototypical protein lyzozyme using the transmitted beam; and photoexcited spin transition dynamics studies of an iron spincrossover system, iron(II) tris(2,20-bipyridine) in water via femtosecond time-resolved X-ray Absorption Near-Edge Spectroscopy (XANES) measurement using the Braggreflected beam
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