Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST

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Abstract

PIST [PDZ (PSD-95, Discs-large and ZO-1) protein interacting specifically with TC10] functions as a regulator of membrane trafficking with Rab6A. Recently, the involvement of the fusion of PIST with ROS1 in cancer development has been identified. In this study, the coiled-coil domain of PIST, which is the domain responsible for interaction with Rab6A and fusion with ROS1, corresponding to amino acids 29-133, was overexpressed in Escherichia coli using engineered C-terminal His tags. The coiled-coil domain of PIST was then purified to homogeneity and crystallized at 293 K. Finally, X-ray diffraction data were collected to a resolution of 4.0 Å from a crystal belonging to the hexagonal space group P6222 or P6422, with unit-cell parameters a = b = 85.19, c = 240.09 Å, γ = 120.00°. © 2013 International Union of Crystallography.

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Shin, Y. C., Seo, E. K., Jeon, J. H., & Park, H. H. (2013). Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 69(4), 468–471. https://doi.org/10.1107/S1744309113007082

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