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Proceedings Paper

Time-resolved crystallography on p21H-ras
Author(s): Axel J. Scheidig
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Paper Abstract

The small GTP-binding protein p21H-ras was one of the first systems whose GTPase reaction was monitored by time-resolved crystallography. Numerous experiments have been carried out to establish the experimental design. The different parameters which needed to be optimized range from the stereochemistry of the photolabile protecting group of GTP, mutants of p21H-ras, crystallization conditions, crystal size and photolysis conditions. Using this approach we were able to determine two intermediate structures of unstable p21H- ras:GTP. In addition, we could map regions of p21H-ras which display high dynamic behavior during the reaction. This short report will summarize the time-resolved diffraction experiments on p21H-ras and the results that have been obtained so far. I would like to introduce this report with general aspects of time-resolved x-ray experiments and highlight these with a few recent developments on this field (without the intention of complete coverage) which provide important criteria for the design and the strategy of new experiments.

Paper Details

Date Published: 1 September 1995
PDF: 12 pages
Proc. SPIE 2521, Time-Resolved Electron and X-Ray Diffraction, (1 September 1995); doi: 10.1117/12.218361
Show Author Affiliations
Axel J. Scheidig, Max-Planck-Institut fuer Molekulare Physiologie (Germany)

Published in SPIE Proceedings Vol. 2521:
Time-Resolved Electron and X-Ray Diffraction
Peter M. Rentzepis, Editor(s)

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