Subnanosecond-Resolved X-ray Diffraction at the SPring-8 High Flux Beamline BL40XU
- SPring-8/RIKEN, Mikazuki, Hyogo 679-5148 (Japan)
- SPring-8/JASRI, Mikazuki, Hyogo 679-5198 (Japan)
We present subnanosecond-resolved X-ray diffraction experiments at the SPring-8 high flux beamline BL40XU by use of time structure of synchrotron radiation. A phase-locked mechanical chopper (x-ray pulse selector), which is made by Forschungszentrum Juelich, has minimum opening time of 400 nanoseconds and generates single-bunch x-ray pulse trains with variable intervals of 1-2 millisecond (0.5-1 kHz) depending on the rotation speed and with the x-ray pulse duration of {approx} 30 picoseconds from the hybrid bunch mode (D-mode) of the SPring-8 ring operation. The interval of pulse trains is further expanded to more than 1 second by another slower shutter, if necessary. The pulse train is applicable to time-resolved diffraction experiments with both monochromatic and pink beams. An observed Laue data set from lysozyme crystal showed sufficient quality to refine the protein structure at 1.9 A resolution. A 10-nanosecond pulse from a Nd:YAG laser initiating photoreaction in a crystal can be synchronized with the X-ray pulse. Installation of a mode-locked Ti:sapphire laser/regenerative amplifier system which has a pulse duration of {approx} 2 picoseconds for further pump-probe experiments is also planed.
- OSTI ID:
- 20652887
- Journal Information:
- AIP Conference Proceedings, Journal Name: AIP Conference Proceedings Journal Issue: 1 Vol. 705; ISSN APCPCS; ISSN 0094-243X
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
AMPLIFIERS
BEAM BUNCHING
CRYSTALS
ELECTRON DENSITY
FORSCHUNGSZENTRUM JUELICH
HZ RANGE
LYSOZYME
MONOCHROMATIC RADIATION
NEODYMIUM LASERS
PROBES
PROTEIN STRUCTURE
PULSES
ROTATION
SAPPHIRE
SPRING-8 STORAGE RING
SYNCHROTRON RADIATION
TIME RESOLUTION
TIMING CIRCUITS
VELOCITY
X-RAY DIFFRACTION