Time-resolved crystallography on p21H-ras

Axel J. Scheidig

doi:10.1117/12.218361

1 September 1995 Time-resolved crystallography on p21^H-ras

Axel J. Scheidig

Proceedings Volume 2521, Time-Resolved Electron and X-Ray Diffraction; (1995) https://doi.org/10.1117/12.218361
Event: SPIE's 1995 International Symposium on Optical Science, Engineering, and Instrumentation, 1995, San Diego, CA, United States

Abstract

The small GTP-binding protein p21^H-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 p21^H-ras, crystallization conditions, crystal size and photolysis conditions. Using this approach we were able to determine two intermediate structures of unstable p21^{H- ras}:GTP. In addition, we could map regions of p21^H-ras which display high dynamic behavior during the reaction. This short report will summarize the time-resolved diffraction experiments on p21^H-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.

Citation Download Citation

Axel J. Scheidig "Time-resolved crystallography on p21^H-ras", Proc. SPIE 2521, Time-Resolved Electron and X-Ray Diffraction, (1 September 1995); https://doi.org/10.1117/12.218361

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