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Article: Purification, crystallization and preliminary X-ray diffraction analysis of the HMG domain of Sox17 in complex with DNA

TitlePurification, crystallization and preliminary X-ray diffraction analysis of the HMG domain of Sox17 in complex with DNA
Authors
KeywordsSox17
LAMA1
HMG domains
Issue Date2008
Citation
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 2008, v. 64, n. 12, p. 1184-1187 How to Cite?
AbstractSox17 is a member of the SRY-related high-mobility group (HMG) of transcription factors that have been shown to direct endodermal differentiation in early mammalian development. The LAMA1 gene encoding the α-chain of laminin-1 has been reported to be directly bound and regulated by Sox17. This paper describes the details of initial crystallization attempts with the HMG domain of mouse Sox17 (mSox17-HMG) with a 16-mer DNA element derived from the LAMA1 enhancer and optimization strategies to obtain a better diffracting crystal. The best diffracting crystal was obtained in a condition containing 0.1 M Tris-HCl pH 7.4, 0.2 M MgCl 2 , 30% PEG 3350 using the hanging-drop vapour-diffusion method. A highly redundant in-house data set was collected to 2.75 Å resolution with 99% completeness. The presence of the mSox17-HMG-DNA complex within the crystals was confirmed and Matthews analysis indicated the presence of one complex per asymmetric unit. © International Union of Crystallography 2008.
Persistent Identifierhttp://hdl.handle.net/10722/253103
ISSN
2020 Impact Factor: 1.056
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorNg, Calista Keow Leng-
dc.contributor.authorPalasingam, Paaventhan-
dc.contributor.authorVenkatachalam, Rajakannan-
dc.contributor.authorBaburajendran, Nithya-
dc.contributor.authorCheng, Jason-
dc.contributor.authorJauch, Ralf-
dc.contributor.authorKolatkar, Prasanna R.-
dc.date.accessioned2018-05-11T05:38:36Z-
dc.date.available2018-05-11T05:38:36Z-
dc.date.issued2008-
dc.identifier.citationActa Crystallographica Section F: Structural Biology and Crystallization Communications, 2008, v. 64, n. 12, p. 1184-1187-
dc.identifier.issn1744-3091-
dc.identifier.urihttp://hdl.handle.net/10722/253103-
dc.description.abstractSox17 is a member of the SRY-related high-mobility group (HMG) of transcription factors that have been shown to direct endodermal differentiation in early mammalian development. The LAMA1 gene encoding the α-chain of laminin-1 has been reported to be directly bound and regulated by Sox17. This paper describes the details of initial crystallization attempts with the HMG domain of mouse Sox17 (mSox17-HMG) with a 16-mer DNA element derived from the LAMA1 enhancer and optimization strategies to obtain a better diffracting crystal. The best diffracting crystal was obtained in a condition containing 0.1 M Tris-HCl pH 7.4, 0.2 M MgCl 2 , 30% PEG 3350 using the hanging-drop vapour-diffusion method. A highly redundant in-house data set was collected to 2.75 Å resolution with 99% completeness. The presence of the mSox17-HMG-DNA complex within the crystals was confirmed and Matthews analysis indicated the presence of one complex per asymmetric unit. © International Union of Crystallography 2008.-
dc.languageeng-
dc.relation.ispartofActa Crystallographica Section F: Structural Biology and Crystallization Communications-
dc.subjectSox17-
dc.subjectLAMA1-
dc.subjectHMG domains-
dc.titlePurification, crystallization and preliminary X-ray diffraction analysis of the HMG domain of Sox17 in complex with DNA-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1107/S1744309108038724-
dc.identifier.pmid19052383-
dc.identifier.scopuseid_2-s2.0-57349105289-
dc.identifier.volume64-
dc.identifier.issue12-
dc.identifier.spage1184-
dc.identifier.epage1187-
dc.identifier.eissn1744-3091-
dc.identifier.isiWOS:000261198700028-
dc.identifier.issnl1744-3091-

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