Journal Article

PUBDB-2021-04056

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Pink-beam serial femtosecond crystallography for accurate structure-factor determination at an X-ray free-electron laser

Nass, K. (Corresponding author) ; Bacellar, C. ; Cirelli, C. ; Dworkowski, F. ; Gevorkov, Y.Extern*XFEL.EU* ; James, D. ; Johnson, P. J. M. ; Kekilli, D. ; Knopp, G. ; Martiel, I. ; Ozerov, D. ; Tolstikova, A.XFEL.EU*DESY* ; Vera, L. ; Weinert, T. ; Yefanov, O.CFEL*XFEL.EU*DESY* ; Standfuss, J. ; Reiche, S. ; Milne, C. J.

2021
Chester

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Please use a persistent id in citations: doi:10.1107/S2052252521008046  doi:10.3204/PUBDB-2021-04056

Abstract: Serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs) enables essentially radiation-damage-free macromolecular structure determination using microcrystals that are too small for synchrotron studies. However, SFX experiments often require large amounts of sample in order to collect highly redundant data where some of the many stochastic errors can be averaged out to determine accurate structure-factor amplitudes. In this work, the capability of the Swiss X-ray free-electron laser (SwissFEL) was used to generate large-bandwidth X-ray pulses [$Δλ/λ$ = 2.2% full width at half-maximum (FWHM)], which were applied in SFX with the aim of improving the partiality of Bragg spots and thus decreasing sample consumption while maintaining the data quality. Sensitive data-quality indicators such as anomalous signal from native thaumatin micro-crystals and de novo phasing results were used to quantify the benefits of using pink X-ray pulses to obtain accurate structure-factor amplitudes. Compared with data measured using the same setup but using X-ray pulses with typical quasi-monochromatic XFEL bandwidth (Δλ/λ = 0.17% FWHM), up to fourfold reduction in the number of indexed diffraction patterns required to obtain similar data quality was achieved. This novel approach, pink-beam SFX, facilitates the yet underutilized de novo structure determination of challenging proteins at XFELs, thereby opening the door to more scientific breakthroughs.

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Contributing Institute(s):

1. CFEL-Coherent X-Ray Imaging (FS-CFEL-1)

Research Program(s):

1. 633 - Life Sciences – Building Blocks of Life: Structure and Function (POF4-633) (POF4-633)

Experiment(s):

1. No specific instrument

Appears in the scientific report 2021

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