author_facet Shin, Young-Cheul
Seo, Eun Kyoung
Jeon, Ju-Hong
Park, Hyun Ho
Shin, Young-Cheul
Seo, Eun Kyoung
Jeon, Ju-Hong
Park, Hyun Ho
author Shin, Young-Cheul
Seo, Eun Kyoung
Jeon, Ju-Hong
Park, Hyun Ho
spellingShingle Shin, Young-Cheul
Seo, Eun Kyoung
Jeon, Ju-Hong
Park, Hyun Ho
Acta Crystallographica Section F Structural Biology and Crystallization Communications
Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST
Condensed Matter Physics
Genetics
Biochemistry
Structural Biology
Biophysics
author_sort shin, young-cheul
spelling Shin, Young-Cheul Seo, Eun Kyoung Jeon, Ju-Hong Park, Hyun Ho 1744-3091 International Union of Crystallography (IUCr) Condensed Matter Physics Genetics Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1107/s1744309113007082 <jats:p>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<jats:italic>Escherichia coli</jats:italic>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<jats:italic>P</jats:italic>6<jats:sub>2</jats:sub>22 or<jats:italic>P</jats:italic>6<jats:sub>4</jats:sub>22, with unit-cell parameters<jats:italic>a</jats:italic>=<jats:italic>b</jats:italic>= 85.19,<jats:italic>c</jats:italic>= 240.09 Å, γ = 120.00°.</jats:p> Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST Acta Crystallographica Section F Structural Biology and Crystallization Communications
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series Acta Crystallographica Section F Structural Biology and Crystallization Communications
source_id 49
title Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST
title_unstemmed Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST
title_full Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST
title_fullStr Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST
title_full_unstemmed Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST
title_short Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST
title_sort crystallization and preliminary x-ray crystallographic studies of the coiled-coil domain of pist
topic Condensed Matter Physics
Genetics
Biochemistry
Structural Biology
Biophysics
url http://dx.doi.org/10.1107/s1744309113007082
publishDate 2013
physical 468-471
description <jats:p>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<jats:italic>Escherichia coli</jats:italic>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<jats:italic>P</jats:italic>6<jats:sub>2</jats:sub>22 or<jats:italic>P</jats:italic>6<jats:sub>4</jats:sub>22, with unit-cell parameters<jats:italic>a</jats:italic>=<jats:italic>b</jats:italic>= 85.19,<jats:italic>c</jats:italic>= 240.09 Å, γ = 120.00°.</jats:p>
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author Shin, Young-Cheul, Seo, Eun Kyoung, Jeon, Ju-Hong, Park, Hyun Ho
author_facet Shin, Young-Cheul, Seo, Eun Kyoung, Jeon, Ju-Hong, Park, Hyun Ho, Shin, Young-Cheul, Seo, Eun Kyoung, Jeon, Ju-Hong, Park, Hyun Ho
author_sort shin, young-cheul
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description <jats:p>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<jats:italic>Escherichia coli</jats:italic>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<jats:italic>P</jats:italic>6<jats:sub>2</jats:sub>22 or<jats:italic>P</jats:italic>6<jats:sub>4</jats:sub>22, with unit-cell parameters<jats:italic>a</jats:italic>=<jats:italic>b</jats:italic>= 85.19,<jats:italic>c</jats:italic>= 240.09 Å, γ = 120.00°.</jats:p>
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spelling Shin, Young-Cheul Seo, Eun Kyoung Jeon, Ju-Hong Park, Hyun Ho 1744-3091 International Union of Crystallography (IUCr) Condensed Matter Physics Genetics Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1107/s1744309113007082 <jats:p>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<jats:italic>Escherichia coli</jats:italic>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<jats:italic>P</jats:italic>6<jats:sub>2</jats:sub>22 or<jats:italic>P</jats:italic>6<jats:sub>4</jats:sub>22, with unit-cell parameters<jats:italic>a</jats:italic>=<jats:italic>b</jats:italic>= 85.19,<jats:italic>c</jats:italic>= 240.09 Å, γ = 120.00°.</jats:p> Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST Acta Crystallographica Section F Structural Biology and Crystallization Communications
spellingShingle Shin, Young-Cheul, Seo, Eun Kyoung, Jeon, Ju-Hong, Park, Hyun Ho, Acta Crystallographica Section F Structural Biology and Crystallization Communications, Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST, Condensed Matter Physics, Genetics, Biochemistry, Structural Biology, Biophysics
title Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST
title_full Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST
title_fullStr Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST
title_full_unstemmed Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST
title_short Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST
title_sort crystallization and preliminary x-ray crystallographic studies of the coiled-coil domain of pist
title_unstemmed Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST
topic Condensed Matter Physics, Genetics, Biochemistry, Structural Biology, Biophysics
url http://dx.doi.org/10.1107/s1744309113007082