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Time-resolved crystallography on H-ras p21

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Scheidig,  Axel J.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Pai,  Emil F.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Schlichting,  Ilme
Photoreceptors, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Wittinghofer,  Alfred
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Goody,  Roger S.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Scheidig, A. J., Pai, E. F., Schlichting, I., Corrie, J. E. T., Reid, G. P., Wittinghofer, A., et al. (1992). Time-resolved crystallography on H-ras p21. Philosophical Transactions of the Royal Society A, 340(1657), 263-272. Retrieved from https://www.jstor.org/stable/53892?seq=1#metadata_info_tab_contents.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-AB37-B
Abstract
We describe here the results obtained to date on a project aimed at characterizing the changes occurring in the protein product (p21) of the H-ras proto-oncogene during and as a result of hydrolysis of GTP at its active site. The approach used involves crystallization of p21 with a photosensitive precursor of GTP (caged GTP) at the active site followed by generation of GTP by photolysis and collection of X-ray diffraction data using the Laue method at a synchrotron source. The structure of p21 complexed with a single diastereomer of caged GTP is presented here. In contrast to crystals obtained with mixed diastereomers, the nucleotide appears to bind in a manner which is very similar to that of other guanine nucleotides (GDP, GTP, GppNHp). The current state of time resolved structural experiments using these crystals is presented.