Dresden 2017 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 56: Protein Structure and Dynamics
BP 56.8: Vortrag
Donnerstag, 23. März 2017, 17:00–17:15, SCH A251
Femtosecond Time-Resolved Dynamics in Myoglobin observed with an XFEL — •Henrike M. Müller-Werkmeister1,2, Helen M. Ginn3, Anling Kuo4, Antoine Sarracini2, Helen Duyvesteyn3, Sascha W. Epp1, Darren Sherrell5, Shigeki Owada6, Olivier Pare-Labrosse2, Saeed Oghbaey2, Jessica Besaw2, Yoshiaki Kumagai7, Kensuke Tono6, Yinpeng Zhong1, Koji Motomura7, Bryan T. Eger2, Alexander Marx1, Arwen R. Pearson8, Robin L. Owen5, Kiyoshi Ueda7, David I. Stuart3, 5, Oliver P. Ernst4, and R. J. Dwayne Miller1,2 — 1Max-Planck-Institute for Structure and Dynamics of Matter, Hamburg, Germany — 2Departments of Chemistry and Physics, University of Toronto, Canada — 3University of Oxford, United Kingdom — 4Department of Biochemistry, University of Toronto, Canada — 5Diamond Light Source, Didcot, United Kingdom — 6SACLA, RIKEN Spring-8 Center, Hyogo, Japan — 7Tohoku University, Sendai, Japan — 8Hamburg University, The Hamburg Center for Ultrafast Imaging, Germany
Here we present recent results from femtosecond time-resolved serial crystallography experiments performed at the X-Ray free electron laser SACLA. We have studied the ligand dissociation in Myoglobin in the time window between 0 fs and 2 ps under functionally relevant conditions, that is, at low laser excitation conditions to prevent spurious artefacts introduced by multi photon processes. The results provide an unprecedented insight into the ultrafast structural changes right after the ligand dissociation.