Agata Butryn


Agata is a Post-Doctoral Research Associate. She joined XFEL-Hub in October 2016 and is partially based in the Research Complex at Harwell. She was previously at the Ludwig Maximillian University of Munich, Germany, where she obtained her doctoral degree in structural biology.

Tel: +44 (0) 123577 8788

Key Research Area

  1. Research profile
  2. Publications
Research profile -

Current main research interests


Room-temperature serial crystallography

Room-temperature serial crystallography data are of comparable quality and have several advantages over the data collected at cryo-temperatures. In particular, room-temperature structure determination is more physiologically relevant, enables time-resolved investigations of protein kinetics, and reduces crystal handling. This kind of data collection scheme can be performed at XFEL sources, but due to the scarcity of the beamtime available at XFEL facilities, serial data collection is now done also at synchrotron sources in a routine manner. Serial crystallography approach requires continuous replenishment of the sample, as most of the time only one diffraction pattern is obtained from a single crystal. This requires development of novel and versatile sample delivery methods and work on improved data processing pipelines. As a part of the XFEL-Hub team I am involved in establishing serial data collection schemes at Diamond, e.g. high-viscosity extruder system, which is also regularly used at SACLA and LCLS XFEL facilities. By that we enable users to test their samples in an XFEL-like environment (for example before submitting their XFEL beamtime proposals) or to collect complete room-temperature datasets from microcrystals.

 Synthesis of cyclic nucleotides

My work at the Research Complex at Harwell is focused on structural analysis of proteins involved in the synthesis of cyclic and di-cyclic nucleotides. I am interested in time-resolved X-ray analysis of the reaction catalyzed by these classes of enzymes, in particular where synthesis of the second messenger is linked to a photoinduced reaction cycle of the internal chromophore in the sensory domain.



Publications - +


Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1. Butryn A, Schuller JM, Stoehr G, Runge-Wollmann P, Förster F, Auble DT, Hopfner KP. Elife. 2015 Aug 10;4. doi: 10.7554/eLife.07432.

Serendipitous crystallization and structure determination of cyanase (CynS) from Serratia proteamaculans. Butryn A, Stoehr G, Linke-Winnebeck C, Hopfner KP. Acta Crystallogr F Struct Biol Commun. 2015 Apr;71(Pt 4):471-6. doi: 10.1107/S2053230X15004902.

Structure and mechanism of the Swi2/Snf2 remodeller Mot1 in complex with its substrate TBP. Wollmann P, Cui S, Viswanathan R, Berninghausen O, Wells MN, Moldt M, Witte G, Butryn A, Wendler P, Beckmann R, Auble DT, Hopfner KP. Nature. 2011 Jul 6;475(7356):403-7. doi: 10.1038/nature10215.