» Articles » PMID: 31074429

The Single Particles, Clusters and Biomolecules and Serial Femtosecond Crystallography Instrument of the European XFEL: Initial Installation

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.

Citing Articles

Present and future structural biology activities at DESY and the European XFEL.

Oberthur D, Hakanpaa J, Chatziefthymiou S, Pompidor G, Bean R, Chapman H J Synchrotron Radiat. 2025; 32(Pt 2):474-485.

PMID: 39964790 PMC: 11892905. DOI: 10.1107/S1600577525000669.


Development of the Nanobeam X-ray Experiments instrument at PAL-XFEL.

Kim J, Hyun H, Kim S, Hwang S, Kim M, Jang D J Synchrotron Radiat. 2025; 32(Pt 2):466-473.

PMID: 39937517 PMC: 11892900. DOI: 10.1107/S1600577525000426.


Real-time analysis of liquid jet sample delivery stability for an X-ray free-electron laser using machine vision.

Patel J, Round A, de Wijn R, Vakili M, Giovanetti G, Melo D J Appl Crystallogr. 2024; 57(Pt 6):1859-1870.

PMID: 39628876 PMC: 11611288. DOI: 10.1107/S1600576724009853.


Development of MHz X-ray phase contrast imaging at the European XFEL.

Koliyadu J, Mosko D, Asimakopoulou E, Bellucci V, Birnsteinova S, Bean R J Synchrotron Radiat. 2024; 32(Pt 1):17-28.

PMID: 39565194 PMC: 11708855. DOI: 10.1107/S160057752400986X.


Crystal structure of a bacterial photoactivated adenylate cyclase determined by serial femtosecond and serial synchrotron crystallography.

Kapetanaki S, Coquelle N, von Stetten D, Byrdin M, Rios-Santacruz R, Bean R IUCrJ. 2024; 11(Pt 6):991-1006.

PMID: 39470573 PMC: 11533990. DOI: 10.1107/S2052252524010170.


References
1.
Andreasson J, Martin A, Liang M, Timneanu N, Aquila A, Wang F . Automated identification and classification of single particle serial femtosecond X-ray diffraction data. Opt Express. 2014; 22(3):2497-510. DOI: 10.1364/OE.22.002497. View

2.
Rollen K, Granzin J, Batra-Safferling R, Stadler A . Small-angle X-ray scattering study of the kinetics of light-dark transition in a LOV protein. PLoS One. 2018; 13(7):e0200746. PMC: 6047819. DOI: 10.1371/journal.pone.0200746. View

3.
Graceffa R, Nobrega R, Barrea R, Kathuria S, Chakravarthy S, Bilsel O . Sub-millisecond time-resolved SAXS using a continuous-flow mixer and X-ray microbeam. J Synchrotron Radiat. 2013; 20(Pt 6):820-5. PMC: 3795536. DOI: 10.1107/S0909049513021833. View

4.
Roedig P, Ginn H, Pakendorf T, Sutton G, Harlos K, Walter T . High-speed fixed-target serial virus crystallography. Nat Methods. 2017; 14(8):805-810. PMC: 5588887. DOI: 10.1038/nmeth.4335. View

5.
Aquila A, Barty A, Bostedt C, Boutet S, Carini G, dePonte D . The linac coherent light source single particle imaging road map. Struct Dyn. 2016; 2(4):041701. PMC: 4711616. DOI: 10.1063/1.4918726. View