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@ARTICLE{Guenther:637447,
      author       = {Guenther, Sebastian and Fischer, Pontus and Galchenkova,
                      Marina and Falke, Sven and Reinke, Patrick and Thekku Veedu,
                      Sreevidya and Rodrigues, Ana Carolina and Senst, Johanna
                      Maria and Elinjikkal, Daniel and Gumprecht, Lars and Meyer,
                      Jan and Chapman, Henry N. and Barthelmess, Miriam and
                      Meents, Alke},
      title        = {{R}oom-temperature {X}-ray fragment screening with serial
                      crystallography},
      journal      = {Nature Communications},
      volume       = {16},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Springer Nature},
      reportid     = {PUBDB-2025-03854},
      pages        = {9089},
      year         = {2025},
      note         = {The following grants are not listed in the system and,
                      therefore, I could not select them:- Federal Ministry of
                      Education and Research (BMBF) via the
                      Röntgen-Ångström-Cluster project “X-ray drug design
                      platform” (13K22CHB) and project “conSCIENCE”
                      (16GW0277)- Helmholtz Society: FISVIR and SFragX - Helmholtz
                      Association Impulse and Networking funds
                      InternLabs-0011-HIR3X- Deutsche Forschungsgemeinschaft
                      (DFG): Cluster of Excellence “CUI: Advanced Imaging of
                      Matter” of the—EXC 2056—project ID 390715994},
      abstract     = {Structural insights into protein-ligand interactions are
                      essential for advancing drug development, with
                      macromolecular X-ray crystallography being a cornerstone
                      technique. Commonly X-ray data collection is conducted at
                      cryogenic temperatures to mitigate radiation damage effects.
                      However, this can introduce artifacts not only in the
                      protein conformation but also in protein-ligand
                      interactions. Recent studies highlight the advantages of
                      room-temperature (RT) crystallography in capturing relevant
                      states much closer to physiological temperatures. We have
                      advanced fixed-target serial crystallography to enable
                      high-throughput fragment screening at RT. Here we
                      systematically compare RT fragment screening with
                      conventional single crystal data collection at cryogenic
                      temperature (cryo) of the Fosfomycin-resistance protein A
                      from Klebsiella pneumoniae (FosAKP), an enzyme involved in
                      antibiotic resistance. With RT serial crystallography we
                      achieve resolutions comparable to cryogenic methods and
                      identify a previously unobserved conformational state of the
                      active site, offering additional starting points for drug
                      design. For ligands identified in both screens, temperature
                      did not have an influence on the binding mode of the ligand.
                      But overall, we observed more binders at cryo, both at
                      physiologically relevant and non-relevant sites. With the
                      potential for further automation, RT screening with serial
                      crystallography can advance drug development pipelines by
                      making new conformations of proteins accessible.},
      cin          = {FS-CFEL-1-BMX},
      ddc          = {500},
      cid          = {I:(DE-H253)FS-CFEL-1-BMX-20210408},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633) / 6G3 - PETRA III (DESY) (POF4-6G3)
                      / FS-Proposal: BAG-20230011 (BAG-20230011) / FISCOV - FISCOV
                      Helmholtz large research infrastructures in the fight
                      against epidemic outbreaks (FISCOV) / AIM, DFG project
                      G:(GEPRIS)390715994 - EXC 2056: CUI: Advanced Imaging of
                      Matter (390715994)},
      pid          = {G:(DE-HGF)POF4-633 / G:(DE-HGF)POF4-6G3 /
                      G:(DE-H253)BAG-20230011 / G:(DE-HGF)FISCOV /
                      G:(GEPRIS)390715994},
      experiment   = {EXP:(DE-H253)P-P09-BMX-20230101 /
                      EXP:(DE-H253)P-P11-20150101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1038/s41467-025-64918-6},
      url          = {https://bib-pubdb1.desy.de/record/637447},
}