New insight into the dynamic properties and the active site architecture of H-Ras p21 revealed by X-ray crystallography at very high resolution |
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Authors: | Björn U Klink Axel J Scheidig |
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Institution: | 1.Department of Biophysics, Division of Structural Biology,Saarland University,Homburg/Saar,Germany;2.Zoological Institute, Department of Structural Biology,Christian-Albrechts University of Kiel,Kiel,Germany;3.Division of Structural Biology,Helmholtz Center for Infection Research,Braunschweig,Germany |
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Abstract: | Background In kinetic crystallography, the usually static method of X-ray diffraction is expanded to allow time-resolved analysis of
conformational rearrangements in protein structures. To achieve this, reactions have to be triggered within the protein crystals
of interest, and optical spectroscopy can be used to monitor the reaction state. For this approach, a modified form of H-Ras
p21 was designed which allows reaction initiation and fluorescence readout of the initiated GTPase reaction within the crystalline
state. Rearrangements within the crystallized protein due to the progressing reaction and associated heterogeneity in the
protein conformations have to be considered in the subsequent refinement processes. |
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Keywords: | |
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