Protein-Ligand Interactions pp 115-154

Part of the Methods in Molecular Biology™ book series (MIMB, volume 305) | Cite as

Protein-Ligand Interaction Probed by Time-Resolved Crystallography

  • Marius Schmidt
  • Hyotcherl Ihee
  • Reinhard Pahl
  • Vukica Šrajer

Abstract

Time-resolved (TR) crystallography is a unique method for determining the structures of intermediates in biomolecular reactions. The technique reached its mature stage with the development of the powerful third-generation synchrotron X-ray sources, and the advances in data processing and analysis of timeresolved Laue crystallographic data. A time resolution of 100 ps has been achieved and relatively small structural changes can be detected even from only partial reaction initiation. The remaining challenge facing the application of this technique to a broad range of biological systems is to find an efficient and rapid, system-specific method for the reaction initiation in the crystal. Other frontiers for the technique involve the continued improvement in time resolution and further advances in methods for determining intermediate structures and reaction mechanisms. The time-resolved technique, combined with trapping methods and computational approaches, holds the promise for a complete structure-based description of biomolecular reactions.

Key Words

Time-resolved macromolecular crystallography Laue diffraction intermediate states reaction mechanism SVD 

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Copyright information

© Humana Press Inc., Totowa, NJ 2005

Authors and Affiliations

  • Marius Schmidt
    • 1
  • Hyotcherl Ihee
    • 2
  • Reinhard Pahl
    • 3
  • Vukica Šrajer
    • 4
  1. 1.Department of PhysicsTechnical University of MunichGarchingGermany
  2. 2.Department of Chemistry and School of Molecular ScienceKAISTDaejeonSouth Korea
  3. 3.Consortium for Advanced Radiation SourcesThe University of ChicagoChicago
  4. 4.Consortium for Advanced Radiation Sources and Department of Biochemistry and Molecular BiologyChicago

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