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Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST
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Zeitschriftentitel: | Acta Crystallographica Section F Structural Biology and Crystallization Communications |
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Personen und Körperschaften: | , , , |
In: | Acta Crystallographica Section F Structural Biology and Crystallization Communications, 69, 2013, 4, S. 468-471 |
Format: | E-Article |
Sprache: | Unbestimmt |
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International Union of Crystallography (IUCr)
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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 |
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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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10.1107/s1744309113007082 |
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Physik Biologie Chemie und Pharmazie |
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International Union of Crystallography (IUCr), 2013 |
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International Union of Crystallography (IUCr), 2013 |
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Acta Crystallographica Section F Structural Biology and Crystallization Communications |
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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 |
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container_title | Acta Crystallographica Section F Structural Biology and Crystallization Communications |
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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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physical | 468-471 |
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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 |