Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of a human condensin SMC2 hinge domain with short coiled coils

Kawahara, Kazuki; Nakamura, Shota; Katsu, Yasuhiro; Motooka, Daisuke; Hosokawa, Yuki; Kojima, Yukiko; Matsukawa, Keiko; Takinowaki, Hiroto; Uchiyama, Susumu; Kobayashi, Yuji; Fukui, Kiichi; Ohkubo, Tadayasu

doi:https://doi.org/10.1107/S1744309110028721

Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of a human condensin SMC2 hinge domain with short coiled coils

Kawahara, Kazuki; Nakamura, Shota; Katsu, Yasuhiro et al.

Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 2010, 66(9), 1067-1070

Number of Access:1,942（2025-08-15 01:09 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/78970

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Title	Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of a human condensin SMC2 hinge domain with short coiled coils
Creator	NRID 1000060585058 1000060585058 researchmap permalink 051619 051619 Scopus Author ID 9740512500 9740512500 CreatorName Kawahara, Kazuki
	NRID 1000090432434 1000090432434 ORCID 0000-0003-2058-5942 0000-0003-2058-5942 researchmap permalink nkmrshota nkmrshota Scopus Author ID 35315778200 35315778200 CreatorName Nakamura, Shota
	CreatorName Katsu, Yasuhiro
	NRID 1000010636830 1000010636830 researchmap permalink daisukem daisukem Scopus Author ID 35315737900 35315737900 CreatorName Motooka, Daisuke
	CreatorName Hosokawa, Yuki
	CreatorName Kojima, Yukiko
	CreatorName Matsukawa, Keiko
	CreatorName Takinowaki, Hiroto
	NRID 1000090335381 1000090335381 ORCID 0000-0002-5181-179X 0000-0002-5181-179X researchmap permalink read0090387 read0090387 Scopus Author ID 35429790100 35429790100 CreatorName Uchiyama, Susumu
	NRID 1000020127228 1000020127228 CreatorName Kobayashi, Yuji
	NRID 1000000311770 1000000311770 researchmap permalink read0068600 read0068600 CreatorName Fukui, Kiichi
	NRID 1000090272997 1000090272997 researchmap permalink read0191274 read0191274 Scopus Author ID 7201618682 7201618682 CreatorName Ohkubo, Tadayasu
Subject	condensin complex
	hinge domains
	SMC subunits
Description	Kawahara, K., Nakamura, S., Katsu, Y., Motooka, D., Hosokawa, Y., Kojima, Y., Matsukawa, K., Takinowaki, H., Uchiyama, S., Kobayashi, Y., Fukui, K. & Ohkubo, T. (2010). Acta Cryst. F66, 1067-1070.
Abstract	In higher eukaryotes, the condensin complex, which mainly consists of two structural maintenance of chromosomes (SMC) subunits, SMC2 (CAP-E) and SMC4 (CAP-C), plays a critical role in the formation of higher order chromosome structures during mitosis. Biochemical and electron-microscopic studies have revealed that the SMC2 and SMC4 subunits dimerize through the interaction of their hinge domains, forming a characteristic V-shaped hetero-dimer. However, the details of their function are still not fully understood owing to a lack of structural information at the atomic level. In this study, the human SMC2 hinge domain with short coiled coils was cloned, expressed, purified and crystallized in the orthorhombic space group C222 in native and SeMet-derivatized forms. Because of the poor diffraction properties of these crystals, the mutant Leu68→SeMet was designed and crystallized in order to obtain the experimental phases. The SeMet-derivatized crystals of the mutant belonged to space group P3212, with unit-cell parameters a = b = 128.8, c = 91.4 Å. The diffraction data obtained from a crystal that diffracted to 2.4 Å resolution were suitable for SAD phasing. © 2010 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)	66(9)
Page	1067-1070
Date of Issued	2010-09-01
Language	English
Handle URL	https://hdl.handle.net/11094/78970
eISSN	17443091
NCID	AA12097708
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1107/S1744309110028721
Relation.isIdenticalTo	PMID 20823528
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. 2010, 66(9), p. 1067-1070
DC.title	Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of a human condensin SMC2 hinge domain with short coiled coils
DC.creator	Kawahara, Kazuki
	Nakamura, Shota
	Katsu, Yasuhiro
	Motooka, Daisuke
	Hosokawa, Yuki
	Kojima, Yukiko
	Matsukawa, Keiko
	Takinowaki, Hiroto
	Uchiyama, Susumu
	Kobayashi, Yuji
	Fukui, Kiichi
	Ohkubo, Tadayasu
DC.publisher	International Union of Crystallography
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2010-09-01
DC.identifier	https://doi.org/10.1107/S1744309110028721
DC.subject	condensin complex
	hinge domains
	SMC subunits
DC.description	Kawahara, K., Nakamura, S., Katsu, Y., Motooka, D., Hosokawa, Y., Kojima, Y., Matsukawa, K., Takinowaki, H., Uchiyama, S., Kobayashi, Y., Fukui, K. & Ohkubo, T. (2010). Acta Cryst. F66, 1067-1070.
DCTERMS.abstract	In higher eukaryotes, the condensin complex, which mainly consists of two structural maintenance of chromosomes (SMC) subunits, SMC2 (CAP-E) and SMC4 (CAP-C), plays a critical role in the formation of higher order chromosome structures during mitosis. Biochemical and electron-microscopic studies have revealed that the SMC2 and SMC4 subunits dimerize through the interaction of their hinge domains, forming a characteristic V-shaped hetero-dimer. However, the details of their function are still not fully understood owing to a lack of structural information at the atomic level. In this study, the human SMC2 hinge domain with short coiled coils was cloned, expressed, purified and crystallized in the orthorhombic space group C222 in native and SeMet-derivatized forms. Because of the poor diffraction properties of these crystals, the mutant Leu68→SeMet was designed and crystallized in order to obtain the experimental phases. The SeMet-derivatized crystals of the mutant belonged to space group P3212, with unit-cell parameters a = b = 128.8, c = 91.4 Å. The diffraction data obtained from a crystal that diffracted to 2.4 Å resolution were suitable for SAD phasing. © 2010 International Union of Crystallography All rights reserved.
DC.rights	© International Union of Crystallography
DC.format	78970
citation_title	Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of a human condensin SMC2 hinge domain with short coiled coils
citation_author	Kawahara, Kazuki
	Nakamura, Shota
	Katsu, Yasuhiro
	Motooka, Daisuke
	Hosokawa, Yuki
	Kojima, Yukiko
	Matsukawa, Keiko
	Takinowaki, Hiroto
	Uchiyama, Susumu
	Kobayashi, Yuji
	Fukui, Kiichi
	Ohkubo, Tadayasu
citation_publisher	International Union of Crystallography
citation_language	English
citation_date	2010-09-01
citation_journal_title	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
citation_volume	66
citation_issue	9
citation_firstpage	1067
citation_lastpage	1070
citation_doi	https://doi.org/10.1107/S1744309110028721
citation_pmid	20823528
citation_public_url	https://hdl.handle.net/11094/78970

Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of a human condensin SMC2 hinge domain with short coiled coils

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