Journal Article

PUBDB-2016-06266

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structural enzymology using X-ray free electron lasers

Kupitz, C. ; Olmos, J. L. ; Holl, M. ; Tremblay, L. ; Pande, K.CFEL*DESY* ; Pandey, S. ; Oberthür, D.CFEL*DESY* ; Hunter, M.Extern* ; Liang, M.CFEL*DESY* ; Aquila, A.Extern* ; Tenboer, J. ; Calvey, G. ; Katz, A. ; Chen, Y. ; Wiedorn, M. O.CFEL*DESY* ; Knoska, J.CFEL*DESY* ; Meents, A.DESY* ; Majriani, V. ; Norwood, T. ; Poudyal, I. ; Grant, T.Extern* ; Miller, M. D. ; Xu, W. ; Tolstikova, A.CFEL*DESY* ; Morgan, A.CFEL*DESY* ; Metz, M.CFEL*DESY* ; Martin-Gracia, J. ; Zook, J. D. ; Roy-Chowdhury, S.Extern* ; Coe, J.Extern* ; Nagaratnam, N. ; Meza, D. ; Fromme, R.Extern* ; Basu, S.CFEL*DESY* ; Frank, M.Extern* ; White, T.CFEL*DESY* ; Barty, A.CFEL*DESY* ; Bajt, S.CFEL*DESY* ; Yefanov, O.CFEL*DESY* ; Chapman, H. N.CFEL*DESY* ; Zatsepin, N. ; Nelson, G.Extern* ; Weierstall, U.Extern* ; Spence, J.Extern* ; Schwander, P. ; Pollack, L. ; Fromme, P.Extern* ; Ourmazd, A. ; Phillips, G. N. ; Schmidt, M. (Corresponding author)

2017
AIP Publishing LLC Melville, NY

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Please use a persistent id in citations: doi:10.1063/1.4972069  doi:10.3204/PUBDB-2016-06266

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.

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Contributing Institute(s):

1. CFEL-Coherent X-Ray Imaging (FS-CFEL-1)
2. FS-Arbeitsgruppe (FS-ML)
3. FS-Photon Science (FS-PS)
4. beauftragt von FS-CFEL-1 (ASU)
5. FS-ML (CFEL-XOM)

Research Program(s):

1. 6215 - Soft Matter, Health and Life Sciences (POF3-621) (POF3-621)
2. 05E13GU1 - Entwicklung eines "Serial Femtosecond Crystallography (SFX)"-Messtandes am Europäischen Elektronenlaser XFEL (BMBF-05E13GU1) (BMBF-05E13GU1)
3. 05K13GU7 - Test eines "Serial Femtosecond Crystallography (SFX)"-Messtandes am Europäischen Elektronenlaser XFEL (BMBF-05K13GU7) (BMBF-05K13GU7)
4. VH-VI-419 - Dynamic Pathways in Multidimensional Landscapes (VH-VI-419) (VH-VI-419)
5. Leibniz Preis - Leibiz Programm 2015: Prof. Dr. Henry N. Chapman (DFG-Leibniz-2015-Chapman) (DFG-Leibniz-2015-Chapman)

Experiment(s):

1. Experiments at CFEL
2. Measurement at external facility

Appears in the scientific report 2017

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Database coverage:
; ; ; ; Current Contents - Physical, Chemical and Earth Sciences ; DOAJ Seal ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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