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@ARTICLE{Pandey:462078,
author = {Pandey, Suraj and Bean, Richard and Sato, Tokushi and
Poudyal, Ishwor and Bielecki, Johan and Cruz Villarreal,
Jorvani and Yefanov, Oleksandr and Mariani, Valerio and
White, Thomas A. and Kupitz, Christopher and Hunter, Mark
and Abdellatif, Mohamed H. and Bajt, Saša and Bondar,
Valerii and Echelmeier, Austin and Doppler, Diandra and
Emons, Moritz and Frank, Matthias and Fromme, Raimund and
Gevorkov, Yaroslav and Giovanetti, Gabriele and Jiang, Man
and Kim, Daihyun and Kim, Yoonhee and Kirkwood, Henry and
Klimovskaia, Anna and Knoska, Juraj and Koua, Faisal H. M.
and Letrun, Romain and Lisova, Stella and Maia, Luis and
Mazalova, Victoria and Meza, Domingo and Michelat, Thomas
and Ourmazd, Abbas and Palmer, Guido and Ramilli, Marco and
Schubert, Robin and Schwander, Peter and Silenzi, Alessandro
and Sztuk-Dambietz, Jolanta and Tolstikova, Alexandra and
Chapman, Henry N. and Ros, Alexandra and Barty, Anton and
Fromme, Petra and Mancuso, Adrian P. and Schmidt, Marius},
title = {{D}irect {O}bservation of the {M}echanism of {A}ntibiotic
{R}esistance by {M}ix-and-{I}nject at the {E}uropean {XFEL}},
publisher = {biorXiv},
reportid = {PUBDB-2021-03253},
year = {2020},
note = {Published in Nature Methods as: "Pandey, S., Bean, R.,
Sato, T. et al. Time-resolved serial femtosecond
crystallography at the European XFEL. Nat Methods 17,
73–78 (2020). https://doi.org/10.1038/s41592-019-0628-z"},
abstract = {In this study, we follow the diffusion and buildup of
occupancy of the substrate ceftriaxone in M. tuberculosis
β-lactamase BlaC microcrystals by structural analysis of
the enzyme substrate complex at single millisecond time
resolution. We also show the binding and the reaction of an
inhibitor, sulbactam, on a slower millisecond time scale. We
use the ‘mix-and-inject’ technique to initiate these
reactions by diffusion, and determine the resulting
structures by serial crystallography using ultrafast,
intense X-ray pulses from the European XFEL (EuXFEL)
arriving at MHz repetition rates. Here, we show how to use
the EuXFEL pulse structure to dramatically increase the size
of the data set and thereby the quality and time resolution
of “molecular movies” which unravel ligand binding and
enzymatically catalyzed reactions. This shows the great
potential for the EuXFEL as a tool for biomedically relevant
research, particularly, as shown here, for investigating
bacterial antibiotic resistance.},
cin = {CFEL-I / FS-CFEL-1 / CFEL-XOM},
ddc = {610},
cid = {I:(DE-H253)CFEL-I-20161114 / I:(DE-H253)FS-CFEL-1-20120731
/ I:(DE-H253)CFEL-XOM-20160915},
pnm = {6215 - Soft Matter, Health and Life Sciences (POF3-621) /
Leibniz Preis - Leibiz Programm 2015: Prof. Dr. Henry N.
Chapman (DFG-Leibniz-2015-Chapman) / X-probe - Advanced XFEL
and Synchrotron based Probes of Protein Structure and
Dynamics (637295) / AXSIS - Frontiers in Attosecond X-ray
Science: Imaging and Spectroscopy (609920)},
pid = {G:(DE-HGF)POF3-6215 / G:(DE-H253)DFG-Leibniz-2015-Chapman /
G:(EU-Grant)637295 / G:(EU-Grant)609920},
experiment = {EXP:(DE-H253)XFEL-Exp-20150101},
typ = {PUB:(DE-HGF)25},
doi = {10.1101/2020.11.24.396689},
url = {https://bib-pubdb1.desy.de/record/462078},
}