Femtosecond X-ray free-electron lasers: A new tool for studying nanocrystals and single macromolecules (original) (raw)
Proceedings of the …, 2012
The ultrabright femtosecond X-ray pulses provided by X-ray freeelectron lasers open capabilities for studying the structure and dynamics of a wide variety of systems beyond what is possible with synchrotron sources. Recently, this "probe-before-destroy" approach has been demonstrated for atomic structure determination by serial X-ray diffraction of microcrystals. There has been the question whether a similar approach can be extended to probe the local electronic structure by X-ray spectroscopy. To address this, we have carried out femtosecond X-ray emission spectroscopy (XES) at the Linac Coherent Light Source using redox-active Mn complexes. XES probes the charge and spin states as well as the ligand environment, critical for understanding the functional role of redox-active metal sites. Kβ 1,3 XES spectra of Mn II and Mn 2 III,IV complexes at room temperature were collected using a wavelength dispersive spectrometer and femtosecond X-ray pulses with an individual dose of up to >100 MGy. The spectra were found in agreement with undamaged spectra collected at low dose using synchrotron radiation. Our results demonstrate that the intact electronic structure of redox active transition metal compounds in different oxidation states can be characterized with this shotby-shot method. This opens the door for studying the chemical dynamics of metal catalytic sites by following reactions under functional conditions. The technique can be combined with X-ray diffraction to simultaneously obtain the geometric structure of the overall protein and the local chemistry of active metal sites and is expected to prove valuable for understanding the mechanism of important metalloproteins, such as photosystem II. energy-dispersive XES | Kβ emission lines | femtosecond x-ray spectroscopy T he first X-ray free-electron laser (XFEL) operating in the hard X-ray regime (1), the Linac Coherent Light Source (LCLS), produces ∼5to 400-fs X-ray pulses with up to ∼10 12 photons per pulse at 6-10 keV at a repetition rate of 120 Hz. Each of these X-ray pulses is intense enough to expel multiple electrons from the target, which can lead to a Coulomb explosion that destroys the sample. In a shot-by-shot experiment, data are collected from each pulse before the destruction of the sample, and the sample is replenished after each pulse. The feasibility of this "probebefore-destroy" approach for X-ray crystallography experiments using XFEL pulses was first demonstrated by Chapman et al. with various systems and has subsequently been corroborated by others at the LCLS (2-6).
Analytical Chemistry, 2013
Atomic resolution structures of large biomacromolecular complexes can now be recorded at room temperature from crystals with submicrometer dimensions using intense femtosecond pulses delivered by the world’s largest and most powerful X-ray machine, a laser called the Linac Coherent Light Source. Abundant opportunities exist for the bioanalytical sciences to help extend this revolutionary advance in structural biology to the ultimate goal of recording molecular-movies of noncrystalline biomacromolecules. This Feature will introduce the concept of serial femtosecond crystallography to the nonexpert, briefly review progress to date, and highlight some potential contributions from the analytical sciences.
Generation of femtosecond X-ray pulses via laser–electron beam interaction
Applied Physics B, 2000
The generation of femtosecond X-ray pulses will have important scientific applications by enabling the direct measurement of atomic motion and structural dynamics in condensed matter on the fundamental time scale of a vibrational period. Interaction of femtosecond laser pulses with relativistic electron beams is an effective approach to generating femtosecond pulses of X-rays. In this paper we present recent results from proof-of-principle experiments in which 300 fs pulses are generated from a synchrotron storage ring by using an ultrashort optical pulse to create femtosecond time structure on the stored electron bunch. A previously demonstrated approach for generating femtosecond X-rays via Thomson scattering between terawatt laser pulses and relativistic electrons is reviewed and compared with storage-ring based schemes.
Megahertz data collection from protein microcrystals at an X-ray free-electron laser
Nature communications, 2018
X-ray free-electron lasers (XFELs) enable novel experiments because of their high peak brilliance and femtosecond pulse duration. However, non-superconducting XFELs offer repetition rates of only 10-120 Hz, placing significant demands on beam time and sample consumption. We describe serial femtosecond crystallography experiments performed at the European XFEL, the first MHz repetition rate XFEL, delivering 1.128 MHz X-ray pulse trains at 10 Hz. Given the short spacing between pulses, damage caused by shock waves launched by one XFEL pulse on sample probed by subsequent pulses is a concern. To investigate this issue, we collected data from lysozyme microcrystals, exposed to a ~15 μm XFEL beam. Under these conditions, data quality is independent of whether the first or subsequent pulses of the train were used for data collection. We also analyzed a mixture of microcrystals of jack bean proteins, from which the structure of native, magnesium-containing concanavalin A was determined.