Journal
JOURNAL OF SYNCHROTRON RADIATION
Volume 26, Issue -, Pages 346-357Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1600577519001577
Keywords
X-ray free-electron laser; serial femtosecond crystallography; protein crystallography; time-resolved crystallography; room-temperature crystallography; X-ray FEL
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Funding
- US Department of Energy, Office of Science, Biological and Environmental Research via the SLAC Mesoscale Integrated Biology Pilot Project
- Linac Coherent Light Source (LCLS), SLAC National Accelerator Laboratory - US Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- National Institute of General Medical Sciences (NIGMS)
- National Science Foundation (NSF)
- Howard Hughes Medical Institutes
- US Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- DOE Office of Biological and Environmental Research
- National Institutes of Health, National Institute of General Medical Sciences [P41GM103393]
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The Macromolecular Femtosecond Crystallography (MFX) instrument at the Linac Coherent Light Source (LCLS) is the seventh and newest instrument at the world's first hard X-ray free-electron laser. It was designed with a primary focus on structural biology, employing the ultrafast pulses of X-rays from LCLSat atmospheric conditions to overcome radiation damage limitations in biological measurements. It is also capable of performing various time-resolved measurements. The MFX design consists of a versatile base system capable of supporting multiple methods, techniques and experimental endstations. The primary techniques supported are forward scattering and crystallography, with capabilities for various spectroscopic methods and time-resolved measurements. The location of the MFX instrument allows for utilization of multiplexing methods, increasing user access to LCLS by running multiple experiments simultaneously.
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