Abstract
The new European X-ray Free-Electron Laser is the first X-ray free-electron laser capable of delivering X-ray pulses with a megahertz inter-pulse spacing, more than four orders of magnitude higher than previously possible. However, to date, it has been unclear whether it would indeed be possible to measure high-quality diffraction data at megahertz pulse repetition rates. Here, we show that high-quality structures can indeed be obtained using currently available operating conditions at the European XFEL. We present two complete data sets, one from the well-known model system lysozyme and the other from a so far unknown complex of a β-lactamase from K. pneumoniae involved in antibiotic resistance. This result opens up megahertz serial femtosecond crystallography (SFX) as a tool for reliable structure determination, substrate screening and the efficient measurement of the evolution and dynamics of molecular structures using megahertz repetition rate pulses available at this new class of X-ray laser source.
Highlights
The new European X-ray Free-Electron Laser is the first X-ray free-electron laser capable of delivering X-ray pulses with a megahertz inter-pulse spacing, more than four orders of magnitude higher than previously possible
We present two complete data sets, one from the well-known model system in crystallography, lysozyme and the other from a so far unknown complex of a β-lactamase from Klebsiella pneumoniae involved in antibiotic resistance
Our experiment was conducted at the SPB/SFX instrument of the European XFEL21
Summary
The new European X-ray Free-Electron Laser is the first X-ray free-electron laser capable of delivering X-ray pulses with a megahertz inter-pulse spacing, more than four orders of magnitude higher than previously possible. We present two complete data sets, one from the well-known model system lysozyme and the other from a so far unknown complex of a β-lactamase from K. pneumoniae involved in antibiotic resistance This result opens up megahertz serial femtosecond crystallography (SFX) as a tool for reliable structure determination, substrate screening and the efficient measurement of the evolution and dynamics of molecular structures using megahertz repetition rate pulses available at this new class of X-ray laser source. We present two complete data sets, one from the well-known model system in crystallography, lysozyme and the other from a so far unknown complex of a β-lactamase from Klebsiella pneumoniae involved in antibiotic resistance This result opens up the possibility of SFX structure determination at a far higher rate than previously possible, enabling the efficient measurement of the evolution and dynamics of molecular structures using megahertz repetition rate pulses available at this new class of X-ray laser source. Studying β-lactamase binding is an important demonstration towards both highthroughput substrate screening and future time-resolved diffusion-based SFX experiments in which inhibitor and crystals are mixed on the fly to enable time-resolved structural studies of substrate binding[20]
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