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

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.

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Genre: Journal Article
Alternative Title : Crystallization and preliminary X-ray crystallographic study of the Ras-GTPase-activating domain of human p120GAP

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ProtStructFunctGenet_27_1997_315.pdf (Any fulltext), 91KB
 
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 Creators:
Scheffzek, Klaus1, Author              
Lautwein, Alfred, Author
Scherer, Anna2, Author              
Franken, Sybille1, Author              
Wittinghofer, Alfred1, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: catalytic domain; cross-linking; hanging drop; p21; seeding
 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

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Language(s): eng - English
 Dates: 1996-07-111996-09-031998-12-071997-02-01
 Publication Status: Published in print
 Pages: 4
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 Table of Contents: -
 Rev. Type: Peer
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Title: Proteins: Structure, Function, and Genetics
  Other : Proteins: Struct., Funct., Genet.
Source Genre: Journal
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Publ. Info: New York, NY : John Wiley & Sons
Pages: - Volume / Issue: 27 (2) Sequence Number: - Start / End Page: 315 - 318 Identifier: ISSN: 0887-3585
CoNE: https://pure.mpg.de/cone/journals/resource/954925553393