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@ARTICLE{Schulz:634794,
      author       = {Schulz, Eike and Prester, Andreas and Stetten, David von
                      and Gore, Gargi and Hatton, Caitlin and Bartels, Kim and
                      Leimkohl, Jan-Philipp and Schikora, Hendrik and Ginn, Helen
                      and Tellkamp, Friedjof and Mehrabi, Pedram},
      title        = {{P}robing the modulation of enzyme kinetics by
                      multi-temperature, time-resolved serial crystallography},
      journal      = {Nature Communications},
      volume       = {16},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Springer Nature},
      reportid     = {PUBDB-2025-02618},
      pages        = {6553},
      year         = {2025},
      abstract     = {The vast majority of protein structures are determined at
                      cryogenic temperatures, which are far from physiological
                      conditions. Nevertheless, it is well established that
                      temperature is an essential thermodynamic parameter for
                      understanding the conformational dynamics and functionality
                      of proteins in their native environments. Time-resolved
                      crystallography is a technique that aims to elucidate
                      protein function by examining structural alterations during
                      processes such as ligand binding, catalysis, or allostery.
                      However, this approach is typically conducted under ambient
                      conditions, which may obscure crucial conformational states,
                      that are only visible at physiological temperatures. In this
                      study, we directly address the interplay between protein
                      structure and activity via a method that enables
                      multi-temperature, time-resolved serial crystallography
                      experiments in a temperature window from below 10 °C to
                      above 70 °C. Via this 5D-SSX, time-resolved experiments
                      can now be carried out at physiological temperatures and
                      with long time delays, providing insights into protein
                      function and enzyme catalysis. Our findings demonstrate the
                      temperature-dependent modulation of turnover kinetics for
                      the mesophilic β-lactamase CTX-M-14 and the thermophilic
                      enzyme xylose isomerase, within the full protein structure.},
      cin          = {MPSD / EMBL-User / PETRA III / FS-CFEL-1-DNMX},
      ddc          = {500},
      cid          = {I:(DE-H253)MPSD-20120731 / I:(DE-H253)EMBL-User-20120814 /
                      $I:(DE-H253)PETRA_III-20150811$ /
                      I:(DE-H253)FS-CFEL-1-DNMX-20231108},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633) / 6G3 - PETRA III (DESY) (POF4-6G3)
                      / DFG project G:(GEPRIS)194651731 - EXC 1074: Hamburger
                      Zentrum für ultraschnelle Beobachtung (CUI): Struktur,
                      Dynamik und Kontrolle von Materie auf atomarer Skala
                      (194651731) / DFG project G:(GEPRIS)451079909 - Untersuchung
                      allosterischer Mechanismen durch zeitaufgelöste serielle
                      Synchrotronkristallographie (451079909) / DFG project
                      G:(GEPRIS)458246365 - Zeitaufgelöste Strukturanalysde der
                      extended spectrum Beta-Lactamase CTX-M-14 (458246365) /
                      DynaPLIX - Dynamics of Protein–Ligand Interactions
                      (101071843)},
      pid          = {G:(DE-HGF)POF4-633 / G:(DE-HGF)POF4-6G3 /
                      G:(GEPRIS)194651731 / G:(GEPRIS)451079909 /
                      G:(GEPRIS)458246365 / G:(EU-Grant)101071843},
      experiment   = {EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1038/s41467-025-61631-2},
      url          = {https://bib-pubdb1.desy.de/record/634794},
}