AI Article Synopsis

  • X-ray Free Electron Lasers (XFELs) enhance crystallography by enabling high-quality data collection at unprecedented speeds, particularly with the upcoming megahertz superconducting FELs.
  • Traditional gas dynamic virtual nozzles (GDVNs) are limited due to high sample consumption, making them impractical for some protein studies while a new droplet-on-demand injection method shows promise with significantly lower consumption.
  • The study achieved a collection rate of 150,000 indexed patterns per hour at the European XFEL, yielding impressive lysozyme crystallography data at 1.38 Å resolution, marking a significant advancement in protein structure analysis.

Article Abstract

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.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11026113PMC
http://dx.doi.org/10.1063/4.0000248DOI Listing

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