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Crystallization and preliminary X-ray crystallographic study of the Ras-GTPase-activating domain of human p120GAP

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons95148

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

http://pubman.mpdl.mpg.de/cone/persons/resource/persons95158

Scherer,  Anna
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons92943

Franken,  Sybille
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons95966

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

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Citation

Scheffzek, K., Lautwein, A., Scherer, A., Franken, S., & Wittinghofer, A. (1997). Crystallization and preliminary X-ray crystallographic study of the Ras-GTPase-activating domain of human p120GAP. Proteins: Structure, Function, and Genetics, 27(2), 315-318. doi:10.1002/(SICI)1097-0134(199702)27:2<315:AID-PROT17>3.0.CO;2-P.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-B23D-5
Abstract
Ras-GTPase-activating proteins (Ras-GAPs) are important regulators of the biological activity of Ras within the framework of intracellular communication where GTP-bound Ras (Ras:GTP) is a key signal transducing molecule (Trahey and McCormick, Science 238:542–545, 1987; Boguski and McCormick, Nature 366:643–654, 1993). By accelerating Ras-mediated GTP hydrolysis, Ras-GAPs provide an efficient means to reset the Ras- GTPase cycle to the GDP-bound ‘OFF’-state and terminate the Ras-mediated signal. Here we report the crystallization of the GTPaseactivating domain of the human p120GAP. The crystals belong to the orthorhombic space group symmetry P212121 with unit cell dimensions of a 5 42.2 Å, b 5 55.6 Å, c 5 142.2 Å, a 5 b 5 g 5 90°. Assuming a Matthews parameter of 2.2 Å3/Da, there is one molecule per asymmetric unit. Applying micro-seeding techniques, we grew large single crystals that could not be obtained by other routine methods for crystal improvement. They diffracted to a resolution of approximately 3 Å using X-rays from a rotating anode generator and to better than 1.8 Å in a synchrotron beam. Chemical cross-linking led to reduction of the maximum resolution but to significantly increased stability against mechanical and heavy atom stress