Feasibility and Realization of Single-Pulse Laue Diffraction on Macromolecular Crystals at ESRF

Laue diffraction patterns with an exposure time of ca 60 ps have been acquired at the European Synchrotron Radiation Facility (ESRF) on protein crystals by using the single-bunch mode of the storage ring. A 10 ns laser pulse initiating photodissociation was synchronized with the X-ray pulse. The pot...

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Veröffentlicht in:Journal of synchrotron radiation. - 1994. - 3(1996), Pt 2 vom: 01. März, Seite 65-74
1. Verfasser: Bourgeois, D (VerfasserIn)
Weitere Verfasser: Ursby, T, Wulff, M, Pradervand, C, Legrand, A, Schildkamp, W, Labouré, S, Srajer, V, Teng, T Y, Roth, M, Moffat, K
Format: Aufsatz
Sprache:English
Veröffentlicht: 1996
Zugriff auf das übergeordnete Werk:Journal of synchrotron radiation
Schlagworte:Journal Article
Beschreibung
Zusammenfassung:Laue diffraction patterns with an exposure time of ca 60 ps have been acquired at the European Synchrotron Radiation Facility (ESRF) on protein crystals by using the single-bunch mode of the storage ring. A 10 ns laser pulse initiating photodissociation was synchronized with the X-ray pulse. The potential for a quantitative detection of conformational changes in proteins on the nanosecond timescale with this technique is demonstrated using the example of carbonmonoxymyoglobin, from simulations and real data. The instrumental aspects of the experiment (highly intense X-ray beam, fast shutter system, Laue camera, detector, laser apparatus and synchronization technique) are emphasized
Beschreibung:Date Completed 02.10.2012
Date Revised 16.05.2006
published: Print
Citation Status PubMed-not-MEDLINE
ISSN:0909-0495