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@ARTICLE{Kupitz:316054,
      author       = {Kupitz, Christopher and Olmos, Jose L. and Holl, Mark and
                      Tremblay, Lee and Pande, Kanupriya and Pandey, Suraj and
                      Oberthür, Dominik and Hunter, Mark and Liang, Mengning and
                      Aquila, Andrew and Tenboer, Jason and Calvey, George and
                      Katz, Andrea and Chen, Yujie and Wiedorn, Max O. and Knoska,
                      Juraj and Meents, Alke and Majriani, Valerio and Norwood,
                      Tyler and Poudyal, Ishwor and Grant, Thomas and Miller,
                      Mitchell D. and Xu, Weijun and Tolstikova, Aleksandra and
                      Morgan, Andrew and Metz, Markus and Martin-Gracia, Jose and
                      Zook, James D. and Roy-Chowdhury, Shatabdi and Coe, Jesse
                      and Nagaratnam, Nirupa and Meza, Domingo and Fromme, Raimund
                      and Basu, Shibom and Frank, Matthias and White, Thomas and
                      Barty, Anton and Bajt, Sasa and Yefanov, Oleksandr and
                      Chapman, Henry N. and Zatsepin, Nadia and Nelson, Garrett
                      and Weierstall, Uwe and Spence, John and Schwander, Peter
                      and Pollack, Lois and Fromme, Petra and Ourmazd, Abbas and
                      Phillips, George N. and Schmidt, Marius},
      title        = {{S}tructural enzymology using {X}-ray free electron lasers},
      journal      = {Structural dynamics},
      volume       = {4},
      number       = {4},
      issn         = {2329-7778},
      address      = {Melville, NY},
      publisher    = {AIP Publishing LLC},
      reportid     = {PUBDB-2016-06266},
      pages        = {044003},
      year         = {2017},
      abstract     = {Mix-and-inject serial crystallography (MISC) is a technique
                      designed to image enzyme catalyzed reactions in which small
                      protein crystals are mixed with a substrate just prior to
                      being probed by an X-ray pulse. This approach offers several
                      advantages over flow cell studies. It provides (i) room
                      temperature structures at near atomic resolution, (ii) time
                      resolution ranging from microseconds to seconds, and (iii)
                      convenient reaction initiation. It outruns radiation damage
                      by using femtosecond X-ray pulses allowing damage and
                      chemistry to be separated. Here, we demonstrate that MISC is
                      feasible at an X-ray free electron laser by studying the
                      reaction of M. tuberculosis ß-lactamase microcrystals with
                      ceftriaxone antibiotic solution. Electron density maps of
                      the apo-ß-lactamase and of the ceftriaxone bound form were
                      obtained at 2.8 Å and 2.4 Å resolution, respectively.
                      These results pave the way to study cyclic and non-cyclic
                      reactions and represent a new field of time-resolved
                      structural dynamics for numerous substrate-triggered
                      biological reactions.},
      cin          = {FS-CFEL-1 / FS-ML / FS-PS / ASU / CFEL-XOM},
      ddc          = {530},
      cid          = {I:(DE-H253)FS-CFEL-1-20120731 / I:(DE-H253)FS-ML-20120731 /
                      I:(DE-H253)FS-PS-20131107 / I:(DE-H253)ASU-20151130 /
                      I:(DE-H253)CFEL-XOM-20160915},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621) /
                      05E13GU1 - Entwicklung eines "Serial Femtosecond
                      Crystallography (SFX)"-Messtandes am Europäischen
                      Elektronenlaser XFEL (BMBF-05E13GU1) / 05K13GU7 - Test eines
                      "Serial Femtosecond Crystallography (SFX)"-Messtandes am
                      Europäischen Elektronenlaser XFEL (BMBF-05K13GU7) /
                      VH-VI-419 - Dynamic Pathways in Multidimensional Landscapes
                      (VH-VI-419) / Leibniz Preis - Leibiz Programm 2015: Prof.
                      Dr. Henry N. Chapman (DFG-Leibniz-2015-Chapman)},
      pid          = {G:(DE-HGF)POF3-6215 / G:(DE-H253)BMBF-05E13GU1 /
                      G:(DE-H253)BMBF-05K13GU7 / G:(DE-HGF)VH-VI-419 /
                      G:(DE-H253)DFG-Leibniz-2015-Chapman},
      experiment   = {EXP:(DE-H253)CFEL-Exp-20150101 /
                      EXP:(DE-MLZ)External-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000402004800003},
      pubmed       = {pmid:28083542},
      doi          = {10.1063/1.4972069},
      url          = {https://bib-pubdb1.desy.de/record/316054},
}