Journal article

Single-molecule imaging with longer X-ray laser pulses

Andrew V Martin, Justine K Corso, Carl Caleman, Nicusor Timneanu, Harry M Quiney



During the last five years, serial femtosecond crystallography using X-ray laser pulses has been developed into a powerful technique for determining the atomic structures of protein molecules from micrometre- and sub-micrometre-sized crystals. One of the key reasons for this success is the 'self-gating' pulse effect, whereby the X-ray laser pulses do not need to outrun all radiation damage processes. Instead, X-ray-induced damage terminates the Bragg diffraction prior to the pulse completing its passage through the sample, as if the Bragg diffraction were generated by a shorter pulse of equal intensity. As a result, serial femtosecond crystallography does not need to be performed with pulses..

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Awarded by ARC

Funding Acknowledgements

HMQ and AVM acknowledge funding from the Australian Research Council via its Centres of Excellence programme and AVM acknowledges the ARC Discovery Early Career Researcher Award (DE140100624) programme. CC and NT thank the Swedish Research Foundation, the Rontgen Angstrom Cluster and the Swedish Foundation for Strategic Research for financial support. We are grateful to Jochen Kupper for helpful feedback.