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

Young Cheul Shin, Eun Kyoung Seo, Ju Hong Jeon, Hyun Ho Park

Research output: Contribution to journalArticle

1 Scopus citations


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°.

Original languageEnglish
Pages (from-to)468-471
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number4
StatePublished - 1 Apr 2013


  • PIST
  • Rab small G protein
  • membrane trafficking
  • oncogenic fusion

Cite this