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Mix-and-diffuse serial synchrotron crystallography

By Kenneth R. Beyerlein, Dennis Dierksmeyer, Valerio Mariani, Manuela Kuhn, Iosifina Sarrou, Angelica Ottaviano, Salah Awel, Juraj Knoska, Silje Fuglerud, Olof Jönsson, Stephan Stern, Max Oliver Wiedorn1, Oleksandr Yefanov, Luigi Adriano, Richard Bean, Anja Burkhardt, Pontus Fischer, Michael Heymann, Daniel A. Horke, Katharina E. J. Jungnickel, Elena Kovaleva, Olga Lorbeer, Markus Metz, Jan Meyer, Andrew Morgan, Kanupriya Pande2, Saravanan Panneerselvam, Carolin Seuring, Aleksandra Tolstikova, Julia Lieske, Steve Aplin, Manfred Roessle, Thomas A. White, Henry Chapman1, Alke Meents, Dominik Oberthuer

1. Center for Free-Electron Laser Science 2. University of Wisconsin - Milwaukee

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Category

BioXFEL Publications

Published on

Type

journal-article

Author

Kenneth R. Beyerlein and Dennis Dierksmeyer and Valerio Mariani and Manuela Kuhn and Iosifina Sarrou and Angelica Ottaviano and Salah Awel and Juraj Knoska and Silje Fuglerud and Olof Jönsson and Stephan Stern and Max O. Wiedorn and Oleksandr Yefanov and Luigi Adriano and Richard Bean and Anja Burkhardt and Pontus Fischer and Michael Heymann and Daniel A. Horke and Katharina E. J. Jungnickel and Elena Kovaleva and Olga Lorbeer and Markus Metz and Jan Meyer and Andrew Morgan and Kanupriya Pande and Saravanan Panneerselvam and Carolin Seuring and Aleksandra Tolstikova and Julia Lieske and Steve Aplin and Manfred Roessle and Thomas A. White and Henry N. Chapman and Alke Meents and Dominik Oberthuer

Citation

Beyerlein, K.R. et al., 2017. Mix-and-diffuse serial synchrotron crystallography. IUCrJ, 4(6), pp.769–777. Available at: http://dx.doi.org/10.1107/s2052252517013124.

Abstract

Unravelling the interaction of biological macromolecules with ligands and substrates at high spatial and temporal resolution remains a major challenge in structural biology. The development of serial crystallography methods at X-ray free-electron lasers and subsequently at synchrotron light sources allows new approaches to tackle this challenge. Here, a new polyimide tape drive designed for mix-and-diffuse serial crystallography experiments is reported. The structure of lysozyme bound by the competitive inhibitor chitotriose was determined using this device in combination with microfluidic mixers. The electron densities obtained from mixing times of 2 and 50 s show clear binding of chitotriose to the enzyme at a high level of detail. The success of this approach shows the potential for high-throughput drug screening and even structural enzymology on short timescales at bright synchrotron light sources.

DOI

http://dx.doi.org/10.1107/s2052252517013124