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. 1989 Oct;86(20):7687–7690. doi: 10.1073/pnas.86.20.7687

Biochemical and crystallographic characterization of a complex of c-Ha-ras p21 and caged GTP with flash photolysis.

I Schlichting 1, G Rapp 1, J John 1, A Wittinghofer 1, E F Pai 1, R S Goody 1
PMCID: PMC298135  PMID: 2682619

Abstract

The GTP binding domain of the c-Ha-ras protooncogene product (p21'c) and the corresponding region from an oncogenic mutant form of the protein in which glycine at position 12 has been replaced by valine [p21'(G12V)] have been crystallized with P3-1-(2-nitro)phenylethylguanosine 5'-O-triphosphate (caged GTP) at their active sites. The crystals give x-ray diffraction patterns to a resolution of better than 0.3 nm. Photolysis can be achieved in the crystal, after which GTP hydrolysis takes place at the rate expected from solution studies. Complete x-ray data sets have been obtained for the starting caged-GTP state and the final GDP state after photolysis and hydrolysis, demonstrating the feasibility of time-resolved structural investigations of the process of GTP hydrolysis.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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