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

9Citations
Citations of this article
22Readers
Mendeley users who have this article in their library.
Get full text

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; Bognski 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 GTPase-activating domain of the human p120GAP. The crystals belong to the orthorhombic space group symmetry P212121 with unit cell dimensions of a = 42.2 Å, b = 55.6 Å, c = 142.2 Å, α = β = γ = 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.

Cite

CITATION STYLE

APA

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. https://doi.org/10.1002/(SICI)1097-0134(199702)27:2<315::AID-PROT17>3.0.CO;2-P

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free