Agata Butryn

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Agata is a Beamline Scientist with the XFEL-Hub. She joined the team in October 2016 as a Postdoctoral Research Associate subsequently moving to the Beamline Scientist position in September 2020. She obtained her doctoral degree in structural biology at Ludwig Maximillian University, Munich, Germany in 2015.

Email: agata.butryn@diamond.ac.uk
Tel: +44 (0) 123577 8788

Techniques and Disciplines

  1. Research profile
  2. Publications
Research profile -

 

Room-temperature serial crystallography

Room-temperature (RT) serial crystallography data are of comparable quality and have several advantages over the single-crystal X-ray data collected at cryogenic temperatures. Serial methods overcome the limitations of X-ray-induced radiation damage, enable time-resolved investigations of protein kinetics and reduce crystal handling. Moreover, RT structure determination is more physiologically relevant. Serial RT data collection scheme can be performed at XFEL sources (Serial Femtosecond Crystallography, SFX), 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 Synchrotron Crystallography, SSX). SFX/SSX approaches require continuous replenishment of the sample, as typically only one diffraction pattern is obtained from each 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 the development of serial data collection schemes at Diamond/XFELs (sample testing, sample delivery) as well as direct user support during and after the experiments (data analysis).

 Synthesis of cyclic nucleotides

My work in the wet lab is focused on structural analysis of proteins involved in the synthesis of cyclic and di-cyclic nucleotides - a widespread class of second messengers. I am particularity interested in time-resolved X-ray investigation of signal transduction process, especially where it is linked to a photoinduced reaction cycle of the internal chromophore or first messenger binding to the sensory domain.

Recently, we published the crystal structure of the ligand-bound catalytic domain of rhodopsin-GC (RhGC) from Catenaria anguillulae. RhGC is a guanylate cyclase that synthetizes cGMP in response to light activation. Our study provides important insights into potential mechanisms of GTP/ATP discrimination and regulation of activity of this class of enzymes (Butryn et al., FEBS J., 2019).