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Crystallization and preliminary X-ray structure analysis of thermally unstable p21H-ras guanosine complexes

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Scheffzek,  Klaus
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Kabsch,  Wolfgang
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Schlichting,  Ilme
Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Citation

Scheffzek, K., Kabsch, W., Schlichting, I., Pai, E. F., Lautwein, A., Frech, M., et al. (1994). Crystallization and preliminary X-ray structure analysis of thermally unstable p21H-ras guanosine complexes. Acta Crystallographica. Section D: Biological Crystallography (Copenhagen), 50(4), 521-526. doi:10.1107/S0907444994001253.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-A8FB-9
Abstract
p21 is a small guanine nucleotide binding protein that is involved in intracellular signal transduction. Biochemical data suggest that the presence of the [beta]-phosphate is essential for strong binding of guanine nucleotides to the protein. Guanosine or GMP bind six orders of magnitude more weakly to p21 than GDP or GTP. Moreover, the thermal stability of the protein is dramatically reduced when bound to GMP or guanosine. We have crystallized C-terminally truncated forms of p21H-ras, with guanosine or GMP bound, in the space groups P43212, P21212 and P21. The crystals diffract in the range 2.8-2.2 Å. Details of the crystallization procedures, the characterization of the crystals and preliminary results of structure determination are described. An unexpected electron-density peak was found close to the position of the [beta]-phosphate in the phosphate-binding loop.