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Blanchard , H. et al.

Blanchard , Fontes , Hammet , Pike , Teh , Gleichmann , Gooley , Kobe , Heierhorst ,

Crystallization and preliminary X-ray diffraction studies of FHA domains of Dun1 and Rad53 protein kinases.

Forkhead-associated (FHA) domains are modular protein-protein interaction domains of approximately 130 amino acids present in numerous signalling proteins. FHA-domain-dependent protein interactions are regulated by phosphorylation of target proteins and FHA domains may be multifunctional phosphopeptide-recognition modules. FHA domains of the budding yeast cell-cycle checkpoint protein kinases Dun1p and Rad53p have been crystallized. Crystals of the Dun1-FHA domain exhibit the symmetry of the space group P6(1)22 or P6(5)22, with unit-cell parameters a = b = 127.3, c = 386.3 A; diffraction data have been collected to 3.1 A resolution on a synchrotron source. Crystals of the N-terminal FHA domain (FHA1) of Rad53p diffract to 4.0 A resolution on a laboratory X-ray source and have Laue-group symmetry 4/mmm, with unit-cell parameters a = b = 61.7, c = 104.3 A.[1]

References

Crystallization and preliminary X-ray diffraction studies of FHA domains of Dun1 and Rad53 protein kinases. Blanchard , H., Fontes , M.R., Hammet , A., Pike , B.L., Teh , T., Gleichmann , T., Gooley , P.R., Kobe , B., Heierhorst , J. Acta Crystallogr. D Biol. Crystallogr. (2001) [Pubmed]

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