TY  - JOUR
AU  - Kupitz, Christopher
AU  - Olmos, Jose L.
AU  - Holl, Mark
AU  - Tremblay, Lee
AU  - Pande, Kanupriya
AU  - Pandey, Suraj
AU  - Oberthür, Dominik
AU  - Hunter, Mark
AU  - Liang, Mengning
AU  - Aquila, Andrew
AU  - Tenboer, Jason
AU  - Calvey, George
AU  - Katz, Andrea
AU  - Chen, Yujie
AU  - Wiedorn, Max O.
AU  - Knoska, Juraj
AU  - Meents, Alke
AU  - Majriani, Valerio
AU  - Norwood, Tyler
AU  - Poudyal, Ishwor
AU  - Grant, Thomas
AU  - Miller, Mitchell D.
AU  - Xu, Weijun
AU  - Tolstikova, Aleksandra
AU  - Morgan, Andrew
AU  - Metz, Markus
AU  - Martin-Gracia, Jose
AU  - Zook, James D.
AU  - Roy-Chowdhury, Shatabdi
AU  - Coe, Jesse
AU  - Nagaratnam, Nirupa
AU  - Meza, Domingo
AU  - Fromme, Raimund
AU  - Basu, Shibom
AU  - Frank, Matthias
AU  - White, Thomas
AU  - Barty, Anton
AU  - Bajt, Sasa
AU  - Yefanov, Oleksandr
AU  - Chapman, Henry N.
AU  - Zatsepin, Nadia
AU  - Nelson, Garrett
AU  - Weierstall, Uwe
AU  - Spence, John
AU  - Schwander, Peter
AU  - Pollack, Lois
AU  - Fromme, Petra
AU  - Ourmazd, Abbas
AU  - Phillips, George N.
AU  - Schmidt, Marius
TI  - Structural enzymology using X-ray free electron lasers
JO  - Structural dynamics
VL  - 4
IS  - 4
SN  - 2329-7778
CY  - Melville, NY
PB  - AIP Publishing LLC
M1  - PUBDB-2016-06266
SP  - 044003 
PY  - 2017
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000402004800003
C6  - pmid:28083542
DO  - DOI:10.1063/1.4972069
UR  - https://bib-pubdb1.desy.de/record/316054
ER  -