Crystallization and preliminary X-ray crystallographic analysis of a conserved domain in plants and prokaryotes from Pyrococcus horikoshii OT3

Lin, Linyen; Nakano, Hiroaki; Uchiyama, Susumu; Fujimoto, Satoru; Matsunaga, Sachihiro; Nakamura, Shota; Kobayashi, Yuji; Ohkubo, Tadayasu; Fukui, Kiichi

doi:https://doi.org/10.1107/S1744309105007815

Crystallization and preliminary X-ray crystallographic analysis of a conserved domain in plants and prokaryotes from Pyrococcus horikoshii OT3

Lin, Linyen; Nakano, Hiroaki; Uchiyama, Susumu et al.

Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 2005, 61(4), 414-416

Number of Access:1,387（2025-08-14 23:20 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/78974

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Title	Crystallization and preliminary X-ray crystallographic analysis of a conserved domain in plants and prokaryotes from Pyrococcus horikoshii OT3
Creator	CreatorName Lin, Linyen
	CreatorName Nakano, Hiroaki
	NRID 1000090335381 1000090335381 ORCID 0000-0002-5181-179X 0000-0002-5181-179X researchmap permalink read0090387 read0090387 Scopus Author ID 35429790100 35429790100 CreatorName Uchiyama, Susumu
	CreatorName Fujimoto, Satoru
	NRID 1000040323448 1000040323448 CreatorName Matsunaga, Sachihiro
	NRID 1000090432434 1000090432434 ORCID 0000-0003-2058-5942 0000-0003-2058-5942 researchmap permalink nkmrshota nkmrshota Scopus Author ID 35315778200 35315778200 CreatorName Nakamura, Shota
	NRID 1000020127228 1000020127228 CreatorName Kobayashi, Yuji
	NRID 1000090272997 1000090272997 researchmap permalink read0191274 read0191274 Scopus Author ID 7201618682 7201618682 CreatorName Ohkubo, Tadayasu
	NRID 1000000311770 1000000311770 researchmap permalink read0068600 read0068600 CreatorName Fukui, Kiichi
Subject	Pyrococcus horikoshii
	PPC domain
	AHL1
Description	Lin, L., Nakano, H., Uchiyama, S., Fujimoto, S., Matsunaga, S., Nakamura, S., Kobayashi, Y., Ohkubo, T. & Fukui, K. (2005). Acta Cryst. F61, 414-416.
Abstract	A plant- and prokaryote-conserved domain (PPC) has previously been found in AT-hook motif nuclear localized protein 1 (AHL1) localized in the nuclear matrix of Arabidopsis thaliana (AtAHL1). AtAHL1 has a DNA-binding function. Mutation analyses of AtAHL1 has previously revealed that the hydrophobic region of the PPC domain is essential for its nuclear localization. In this study, the PPC of the hyperthermophilic archaebacterium Pyrococcus horikoshii (PhPPC) was crystallized using the hanging-drop vapour-diffusion method. The crystals belonged to the hexagonal space group P6322, with unit-cell parameters a = b = 53.69, c = 159.2 Å. Data were obtained at 100 K, with diffraction being observed to a resolution of 1.7 Å. A complete data set from crystals of the SeMet-substituted protein was also obtained. © 2005 International Union of Crystallography All rights reserved.
Publisher	International Union of Crystallography
Source Title	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume (Issue)	61(4)
Page	414-416
Date of Issued	2005-12-01
Language	English
Handle URL	https://hdl.handle.net/11094/78974
eISSN	17443091
NCID	AA12097708
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1107/S1744309105007815
Relation.isIdenticalTo	PMID 16511056
Access Rights	open access
CopyRight	© International Union of Crystallography
oaire:version	Version of Record
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCMI Type	Text
DCTERMS.bibliographicCitation	Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2005, 61(4), p. 414-416
DC.title	Crystallization and preliminary X-ray crystallographic analysis of a conserved domain in plants and prokaryotes from Pyrococcus horikoshii OT3
DC.creator	Lin, Linyen
	Nakano, Hiroaki
	Uchiyama, Susumu
	Fujimoto, Satoru
	Matsunaga, Sachihiro
	Nakamura, Shota
	Kobayashi, Yuji
	Ohkubo, Tadayasu
	Fukui, Kiichi
DC.publisher	International Union of Crystallography
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2005-12-01
DC.identifier	https://doi.org/10.1107/S1744309105007815
DC.subject	Pyrococcus horikoshii
	PPC domain
	AHL1
DC.description	Lin, L., Nakano, H., Uchiyama, S., Fujimoto, S., Matsunaga, S., Nakamura, S., Kobayashi, Y., Ohkubo, T. & Fukui, K. (2005). Acta Cryst. F61, 414-416.
DCTERMS.abstract	A plant- and prokaryote-conserved domain (PPC) has previously been found in AT-hook motif nuclear localized protein 1 (AHL1) localized in the nuclear matrix of Arabidopsis thaliana (AtAHL1). AtAHL1 has a DNA-binding function. Mutation analyses of AtAHL1 has previously revealed that the hydrophobic region of the PPC domain is essential for its nuclear localization. In this study, the PPC of the hyperthermophilic archaebacterium Pyrococcus horikoshii (PhPPC) was crystallized using the hanging-drop vapour-diffusion method. The crystals belonged to the hexagonal space group P6322, with unit-cell parameters a = b = 53.69, c = 159.2 Å. Data were obtained at 100 K, with diffraction being observed to a resolution of 1.7 Å. A complete data set from crystals of the SeMet-substituted protein was also obtained. © 2005 International Union of Crystallography All rights reserved.
DC.rights	© International Union of Crystallography
DC.format	78974
citation_title	Crystallization and preliminary X-ray crystallographic analysis of a conserved domain in plants and prokaryotes from Pyrococcus horikoshii OT3
citation_author	Lin, Linyen
	Nakano, Hiroaki
	Uchiyama, Susumu
	Fujimoto, Satoru
	Matsunaga, Sachihiro
	Nakamura, Shota
	Kobayashi, Yuji
	Ohkubo, Tadayasu
	Fukui, Kiichi
citation_publisher	International Union of Crystallography
citation_language	English
citation_date	2005-12-01
citation_journal_title	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
citation_volume	61
citation_issue	4
citation_firstpage	414
citation_lastpage	416
citation_doi	https://doi.org/10.1107/S1744309105007815
citation_pmid	16511056
citation_public_url	https://hdl.handle.net/11094/78974

Crystallization and preliminary X-ray crystallographic analysis of a conserved domain in plants and prokaryotes from Pyrococcus horikoshii OT3

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