Design of the mirror optical systems for coherent diffractive imaging at the SPB/SFX instrument of the European XFEL
TL;DR: In this article, the authors present the design and simulated performance of two state-of-the-art Kirkpatrik-Baez mirror systems that form the primary foci of the single particles, clusters and biomolecules and serial femtosecond crystallography (SPB/SFX) instrument of the European XFEL.
Abstract: The high degree of spatial coherence and extreme pulse energies available at x-ray free electron laser (XFEL) sources naturally support coherent diffractive imaging applications. In order to optimally exploit these unique properties, the optical systems at XFELs must be highly transmissive, focus to appropriate sizes matched to the scale of samples to be investigated and must minimally perturb the wavefront of the XFEL beam. We present the design and simulated performance of two state-of-the-art Kirkpatrik–Baez mirror systems that form the primary foci of the single particles, clusters and biomolecules and serial femtosecond crystallography (SPB/SFX) instrument of the European XFEL. The two systems, presently under construction, will produce 1 μm and 100 nm scale foci across a 3–16 keV photon energy range. Targeted applications include coherent imaging of weakly scattering, often biological, specimens.
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TL;DR: The European XFEL as discussed by the authors is a free-electron laser (FEL) user facility providing soft and hard X-ray FEL radiation to initially six scientific instruments.
Abstract: European XFEL is a free-electron laser (FEL) user facility providing soft and hard X-ray FEL radiation to initially six scientific instruments. Starting user operation in fall 2017 European XFEL will provide new research opportunities to users from science domains as diverse as physics, chemistry, geo- and planetary sciences, materials sciences or biology. The unique feature of European XFEL is the provision of high average brilliance in the soft and hard X-ray regime, combined with the pulse properties of FEL radiation of extreme peak intensities, femtosecond pulse duration and high degree of coherence. The high average brilliance is achieved through acceleration of up to 27,000 electron bunches per second by the super-conducting electron accelerator. Enabling the usage of this high average brilliance in user experiments is one of the major instrumentation drivers for European XFEL. The radiation generated by three FEL sources is distributed via long beam transport systems to the experiment hall where the scientific instruments are located side-by-side. The X-ray beam transport systems have been optimized to maintain the unique features of the FEL radiation which will be monitored using build-in photon diagnostics. The six scientific instruments are optimized for specific applications using soft or hard X-ray techniques and include integrated lasers, dedicated sample environment, large area high frame rate detector(s) and computing systems capable of processing large quantities of data.
260 citations
TL;DR: The results connect the previously explored femtosecond PYP dynamics to timescales accessible at synchrotrons, which opens the door to a wide range of time-resolved studies at the EuXFEL.
Abstract: The European XFEL (EuXFEL) is a 3.4-km long X-ray source, which produces femtosecond, ultrabrilliant and spatially coherent X-ray pulses at megahertz (MHz) repetition rates. This X-ray source has been designed to enable the observation of ultrafast processes with near-atomic spatial resolution. Time-resolved crystallographic investigations on biological macromolecules belong to an important class of experiments that explore fundamental and functional structural displacements in these molecules. Due to the unusual MHz X-ray pulse structure at the EuXFEL, these experiments are challenging. Here, we demonstrate how a biological reaction can be followed on ultrafast timescales at the EuXFEL. We investigate the picosecond time range in the photocycle of photoactive yellow protein (PYP) with MHz X-ray pulse rates. We show that difference electron density maps of excellent quality can be obtained. The results connect the previously explored femtosecond PYP dynamics to timescales accessible at synchrotrons. This opens the door to a wide range of time-resolved studies at the EuXFEL.
100 citations
TL;DR: Strategies for sample delivery of macromolecular crystals at X-ray free-electron lasers are reviewed, covering injection methods, fixed-target approaches and hybrid methods.
Abstract: Highly efficient data-collection methods are required for successful macromolecular crystallography (MX) experiments at X-ray free-electron lasers (XFELs). XFEL beamtime is scarce, and the high peak brightness of each XFEL pulse destroys the exposed crystal volume. It is therefore necessary to combine diffraction images from a large number of crystals (hundreds to hundreds of thousands) to obtain a final data set, bringing about sample-refreshment challenges that have previously been unknown to the MX synchrotron community. In view of this experimental complexity, a number of sample delivery methods have emerged, each with specific requirements, drawbacks and advantages. To provide useful selection criteria for future experiments, this review summarizes the currently available sample delivery methods, emphasising the basic principles and the specific sample requirements. Two main approaches to sample delivery are first covered: (i) injector methods with liquid or viscous media and (ii) fixed-target methods using large crystals or using microcrystals inside multi-crystal holders or chips. Additionally, hybrid methods such as acoustic droplet ejection and crystal extraction are covered, which combine the advantages of both fixed-target and injector approaches.
77 citations
Cites methods from "Design of the mirror optical system..."
...…changer 0.5 mJ at 10 keV Rayonix MX225-HS MPCCD 2–10 fs FWHM 30 Hz, up to 60 Hz European XFEL, Hamburg, Germany SPB/SFX (Altarelli & Mancuso, 2014; Tschentscher et al., 2017; Bean et al., 2016) 1 mm or 0.1 mm upstream, 1 mm downstream Liquid/aerosol/gas injection systems (vacuum), fixed-target…...
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TL;DR: An introduction to the early operational capabilities of the Single Particles, Clusters and Biomolecules and Serial Femtosecond Crystallography scientific instrument at the European X-ray Free Electron Laser facility is presented.
Abstract: The European X-ray Free-Electron Laser (FEL) became the first operational high-repetition-rate hard X-ray FEL with first lasing in May 2017. Biological structure determination has already benefitted from the unique properties and capabilities of X-ray FELs, predominantly through the development and application of serial crystallography. The possibility of now performing such experiments at data rates more than an order of magnitude greater than previous X-ray FELs enables not only a higher rate of discovery but also new classes of experiments previously not feasible at lower data rates. One example is time-resolved experiments requiring a higher number of time steps for interpretation, or structure determination from samples with low hit rates in conventional X-ray FEL serial crystallography. Following first lasing at the European XFEL, initial commissioning and operation occurred at two scientific instruments, one of which is the Single Particles, Clusters and Biomolecules and Serial Femtosecond Crystallography (SPB/SFX) instrument. This instrument provides a photon energy range, focal spot sizes and diagnostic tools necessary for structure determination of biological specimens. The instrumentation explicitly addresses serial crystallography and the developing single particle imaging method as well as other forward-scattering and diffraction techniques. This paper describes the major science cases of SPB/SFX and its initial instrumentation – in particular its optical systems, available sample delivery methods, 2D detectors, supporting optical laser systems and key diagnostic components. The present capabilities of the instrument will be reviewed and a brief outlook of its future capabilities is also described.
73 citations
Kurchatov Institute1, European XFEL2, Uppsala University3, Academy of Sciences of the Czech Republic4, University of Hamburg5, Max Planck Society6, National University of Singapore7, La Trobe University8, Russian Academy of Sciences9, Arizona State University10, University of Wisconsin–Milwaukee11, Pohang University of Science and Technology12, Australian National University13, Royal Institute of Technology14, University at Buffalo15, Heinrich Pette Institute16, Brookhaven National Laboratory17, National Research Nuclear University MEPhI18, Lawrence Berkeley National Laboratory19
TL;DR: The emergence of high repetition-rate X-ray free-electron lasers (XFELs) powered by superconducting accelerator technology enables the measurement of significantly more experimental data per day as discussed by the authors.
Abstract: The emergence of high repetition-rate X-ray free-electron lasers (XFELs) powered by superconducting accelerator technology enables the measurement of significantly more experimental data per day th ...
53 citations
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TL;DR: Computer simulations are used to investigate the structural information that can be recovered from the scattering of intense femtosecond X-ray pulses by single protein molecules and small assemblies and predict that ultrashort, high-intensity X-rays from free-electron lasers that are currently under development will provide a new approach to structural determinations with X- rays.
Abstract: Sample damage by X-rays and other radiation limits the resolution of structural studies on non-repetitive and non-reproducible structures such as individual biomolecules or cells(1). Cooling can slow sample deterioration, but cannot eliminate damage-induc
1,770 citations
University of Hamburg1, Arizona State University2, Uppsala University3, Max Planck Society4, European XFEL5, SLAC National Accelerator Laboratory6, Forschungszentrum Jülich7, Lawrence Livermore National Laboratory8, Lawrence Berkeley National Laboratory9, University of Gothenburg10, Technical University of Berlin11, Swedish University of Agricultural Sciences12
TL;DR: This work offers a new approach to structure determination of macromolecules that do not yield crystals of sufficient size for studies using conventional radiation sources or are particularly sensitive to radiation damage, by using pulses briefer than the timescale of most damage processes.
Abstract: X-ray crystallography provides the vast majority of macromolecular structures, but the success of the method relies on growing crystals of sufficient size. In conventional measurements, the necessary increase in X-ray dose to record data from crystals that are too small leads to extensive damage before a diffraction signal can be recorded(1-3). It is particularly challenging to obtain large, well-diffracting crystals of membrane proteins, for which fewer than 300 unique structures have been determined despite their importance in all living cells. Here we present a method for structure determination where single-crystal X-ray diffraction 'snapshots' are collected from a fully hydrated stream of nanocrystals using femtosecond pulses from a hard-X-ray free-electron laser, the Linac Coherent Light Source(4). We prove this concept with nanocrystals of photosystem I, one of the largest membrane protein complexes(5). More than 3,000,000 diffraction patterns were collected in this study, and a three-dimensional data set was assembled from individual photosystem I nanocrystals (similar to 200 nm to 2 mm in size). We mitigate the problem of radiation damage in crystallography by using pulses briefer than the timescale of most damage processes(6). This offers a new approach to structure determination of macromolecules that do not yield crystals of sufficient size for studies using conventional radiation sources or are particularly sensitive to radiation damage.
1,708 citations
TL;DR: Several conceivable methods for the formation of optical images by x-rays are considered, and a method employing concave mirrors is adopted as the most promising.
Abstract: Several conceivable methods for the formation of optical images by x-rays are considered, and a method employing concave mirrors is adopted as the most promising. A concave spherical mirror receiving radiation at grazing incidence (a necessary arrangement with x-rays) images a point into a line in accordance with a focal length f=Ri/2 where R is the radius of curvature and i the grazing angle. The image is subject to an aberration such that a ray reflected at the periphery of the mirror misses the focal point of central rays by a distance given approximately by S=1.5Mr2/R, where M is the magnification of the image and r is the radius of the mirror face. The theoretically possible resolving power is such as to resolve point objects separated by about 70A, a limit which is independent of the wave-length used. Point images of points and therefore extended images of extended objects may be produced by causing the radiation to reflect from two concave mirrors in series. Sample results are presented.
1,149 citations
TL;DR: In this paper, the FLASH soft X-ray free-electron laser was used to reconstruct a coherent diffraction pattern from a nano-structured nonperiodic object, before destroying it at 60,000 K.
Abstract: Theory predicts that with an ultrashort and extremely bright coherent X-ray pulse, a single diffraction pattern may be recorded from a large macromolecule, a virus, or a cell before the sample explodes and turns into a plasma. Here we report the first experimental demonstration of this principle using the FLASH soft X-ray free-electron laser. An intense 25 fs, 4 x 10{sup 13} W/cm{sup 2} pulse, containing 10{sup 12} photons at 32 nm wavelength, produced a coherent diffraction pattern from a nano-structured non-periodic object, before destroying it at 60,000 K. A novel X-ray camera assured single photon detection sensitivity by filtering out parasitic scattering and plasma radiation. The reconstructed image, obtained directly from the coherent pattern by phase retrieval through oversampling, shows no measurable damage, and extends to diffraction-limited resolution. A three-dimensional data set may be assembled from such images when copies of a reproducible sample are exposed to the beam one by one.
957 citations
Uppsala University1, University of Hamburg2, Aix-Marseille University3, Stanford University4, Swedish University of Agricultural Sciences5, Arizona State University6, Lawrence Berkeley National Laboratory7, Lawrence Livermore National Laboratory8, Max Planck Society9, Technical University of Berlin10
TL;DR: This work shows that high-quality diffraction data can be obtained with a single X-ray pulse from a non-crystalline biological sample, a single mimivirus particle, which was injected into the pulsed beam of a hard-X-ray free-electron laser, the Linac Coherent Light Source.
Abstract: The start-up of the Linac Coherent Light Source (LCLS), the new femtosecond hard X-ray laser facility in Stanford, California, has brought high expectations of a new era for biological imaging. The intense, ultrashort X-ray pulses allow diffraction imaging of small structures before radiation damage occurs. Two papers in this issue of Nature present proof-of-concept experiments showing the LCLS in action. Chapman et al. tackle structure determination from nanocrystals of macromolecules that cannot be grown in large crystals. They obtain more than three million diffraction patterns from a stream of nanocrystals of the membrane protein photosystem I, and assemble a three-dimensional data set for this protein. Seibert et al. obtain images of a non-crystalline biological sample, mimivirus, by injecting a beam of cooled mimivirus particles into the X-ray beam. The start-up of the new femtosecond hard X-ray laser facility in Stanford, the Linac Coherent Light Source, has brought high expectations for a new era for biological imaging. The intense, ultrashort X-ray pulses allow diffraction imaging of small structures before radiation damage occurs. This new capability is tested for the problem of imaging a non-crystalline biological sample. Images of mimivirus are obtained, the largest known virus with a total diameter of about 0.75 micrometres, by injecting a beam of cooled mimivirus particles into the X-ray beam. The measurements indicate no damage during imaging and prove the concept of this imaging technique. X-ray lasers offer new capabilities in understanding the structure of biological systems, complex materials and matter under extreme conditions1,2,3,4. Very short and extremely bright, coherent X-ray pulses can be used to outrun key damage processes and obtain a single diffraction pattern from a large macromolecule, a virus or a cell before the sample explodes and turns into plasma1. The continuous diffraction pattern of non-crystalline objects permits oversampling and direct phase retrieval2. Here we show that high-quality diffraction data can be obtained with a single X-ray pulse from a non-crystalline biological sample, a single mimivirus particle, which was injected into the pulsed beam of a hard-X-ray free-electron laser, the Linac Coherent Light Source5. Calculations indicate that the energy deposited into the virus by the pulse heated the particle to over 100,000 K after the pulse had left the sample. The reconstructed exit wavefront (image) yielded 32-nm full-period resolution in a single exposure and showed no measurable damage. The reconstruction indicates inhomogeneous arrangement of dense material inside the virion. We expect that significantly higher resolutions will be achieved in such experiments with shorter and brighter photon pulses focused to a smaller area. The resolution in such experiments can be further extended for samples available in multiple identical copies.
838 citations