H
Henrike M. Müller-Werkmeister
Researcher at University of Potsdam
Publications - 23
Citations - 501
Henrike M. Müller-Werkmeister is an academic researcher from University of Potsdam. The author has contributed to research in topics: Spin crossover & Infrared spectroscopy. The author has an hindex of 11, co-authored 20 publications receiving 351 citations. Previous affiliations of Henrike M. Müller-Werkmeister include University of Toronto & Goethe University Frankfurt.
Papers
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Journal ArticleDOI
Strategies for sample delivery for femtosecond crystallography
TL;DR: Strategies for sample delivery of macromolecular crystals at X-ray free-electron lasers are reviewed, covering injection methods, fixed-target approaches and hybrid methods.
Journal ArticleDOI
Time-resolved crystallography reveals allosteric communication aligned with molecular breathing
Pedram Mehrabi,Pedram Mehrabi,Pedram Mehrabi,Eike C. Schulz,Raison Dsouza,Raison Dsouza,Henrike M. Müller-Werkmeister,Henrike M. Müller-Werkmeister,Friedjof Tellkamp,R. J. Dwayne Miller,R. J. Dwayne Miller,Emil F. Pai,Emil F. Pai +12 more
TL;DR: Using time-resolved serial synchrotron crystallography, half-of-the-sites reactivity and correlated molecular-breathing motions in the enzyme fluoroacetate dehalogenase are visualized.
Journal ArticleDOI
The hit-and-return system enables efficient time-resolved serial synchrotron crystallography.
Eike C. Schulz,Pedram Mehrabi,Henrike M. Müller-Werkmeister,Henrike M. Müller-Werkmeister,Friedjof Tellkamp,Ajay Jha,W. Stuart,Elke Persch,R. De Gasparo,François Diederich,Emil F. Pai,R.J.D. Miller,R.J.D. Miller,R.J.D. Miller +13 more
TL;DR: A data-collection strategy using a fixed-target crystallography chip allows time-resolved serial synchrotron crystallography experiments to determine enzyme intermediate structures with time resolutions of milliseconds to seconds.
Journal ArticleDOI
A donor–acceptor pair for the real time study of vibrational energy transfer in proteins
TL;DR: This work addresses the requirements for extending this powerful approach to proteins and presents a protein-compatible donor-acceptor pair for the real time investigation of VET, and investigates the performance of the proposed VET pair in a model peptide designed to contain additional characteristic vibrational modes frequently used in infrared spectroscopy of proteins.
Journal ArticleDOI
Structural Dynamics upon Photoexcitation in a Spin Crossover Crystal Probed with Femtosecond Electron Diffraction
Yifeng Jiang,Lai Chung Liu,Henrike M. Müller-Werkmeister,Cheng Lu,Dongfang Zhang,Ryan L. Field,Antoine Sarracini,Gustavo Moriena,Eric Collet,R. J. Dwayne Miller +9 more
TL;DR: The data and refinement calculations indicate the global structural reorganization within 2.3 ps, as the metal-ligand bond distribution narrows during intramolecular vibrational energy redistribution (IVR) driving the intermolecular rearrangement.