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Journal Article

Megahertz serial crystallography

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Heymann,  Michael
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Wiedorn, M. O., Oberthür, D., Bean, R., Schubert, R., Werner, N., Abbey, B., et al. (2018). Megahertz serial crystallography. Nature Communications, 9: 4025. doi:10.1038/s41467-018-06156-7.


Cite as: https://hdl.handle.net/21.11116/0000-0002-F155-E
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.