دورية أكاديمية

Kilohertz droplet-on-demand serial femtosecond crystallography at the European XFEL station FXE.

التفاصيل البيبلوغرافية
العنوان: Kilohertz droplet-on-demand serial femtosecond crystallography at the European XFEL station FXE.
المؤلفون: Perrett, Samuel, Fadini, Alisia, Hutchison, Christopher D. M., Bhattacharya, Sayantan, Morrison, Cade, Turkot, Oleksii, Jakobsen, Mads Bregenholt, Größler, Michael, Licón-Saláiz, José, Griese, Florian, Flewett, Samuel, Valerio, Joana, Schulz, Joachim, Biednov, Mykola, Jiang, Yifeng, Han, Huijong, Yousef, Hazem, Khakhulin, Dmitry, Milne, Christopher, Barty, Anton
المصدر: Structural Dynamics; Mar2024, Vol. 11 Issue 2, p1-12, 12p
مصطلحات موضوعية: PROTEIN fractionation, CRYSTALLOGRAPHY, GAS dynamics, FREE electron lasers, PROTEIN structure, SIGNAL-to-noise ratio
مستخلص: X-ray Free Electron Lasers (XFELs) allow the collection of high-quality serial femtosecond crystallography data. The next generation of megahertz superconducting FELs promises to drastically reduce data collection times, enabling the capture of more structures with higher signal-to-noise ratios and facilitating more complex experiments. Currently, gas dynamic virtual nozzles (GDVNs) stand as the sole delivery method capable of best utilizing the repetition rate of megahertz sources for crystallography. However, their substantial sample consumption renders their use impractical for many protein targets in serial crystallography experiments. Here, we present a novel application of a droplet-on-demand injection method, which allowed operation at 47 kHz at the European XFEL (EuXFEL) by tailoring a multi-droplet injection scheme for each macro-pulse. We demonstrate a collection rate of 150 000 indexed patterns per hour. We show that the performance and effective data collection rate are comparable to GDVN, with a sample consumption reduction of two orders of magnitude. We present lysozyme crystallographic data using the Large Pixel Detector at the femtosecond x-ray experiment endstation. Significant improvement of the crystallographic statistics was made by correcting for a systematic drift of the photon energy in the EuXFEL macro-pulse train, which was characterized from indexing the individual frames in the pulse train. This is the highest resolution protein structure collected and reported at the EuXFEL at 1.38 Å resolution. [ABSTRACT FROM AUTHOR]
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قاعدة البيانات: Complementary Index
الوصف
تدمد:23297778
DOI:10.1063/4.0000248