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Article: Expression, purification and preliminary crystallographic analysis of recombinant human small glutamine-rich tetratricopeptide-repeat protein

TitleExpression, purification and preliminary crystallographic analysis of recombinant human small glutamine-rich tetratricopeptide-repeat protein
Authors
Issue Date2008
PublisherWiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www3.interscience.wiley.com/journal/117982340/home
Citation
Acta Crystallographica Section F: Structural Biology And Crystallization Communications, 2008, v. 64 n. 7, p. 602-604 How to Cite?
AbstractHuman small glutamine-rich tetratricopeptide-repeat protein (hSGT) is a 35 kDa protein implicated in a number of biological processes that include apoptosis, cell division and intracellular cell transport. The tetratricopeptide-repeat (TPR) domain of hSGT has been cloned and expressed in Escherichia coli and purified. Here, the crystallization and preliminary diffraction analysis of the TPR domain of hSGT is reported. X-ray diffraction data were processed to a resolution of 2.4 Å. Crystals belong to space group P21212, with unit-cell parameters a = 67.82, b = 81.93, c = 55.92 Å, α = β = γ = 90°. © International Union of Crystallography 2008.
Persistent Identifierhttp://hdl.handle.net/10722/171768
ISSN
2014 Impact Factor: 0.524
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorDutta, Sen_US
dc.contributor.authorKotaka, Men_US
dc.contributor.authorTan, YJen_US
dc.date.accessioned2012-10-30T06:16:55Z-
dc.date.available2012-10-30T06:16:55Z-
dc.date.issued2008en_US
dc.identifier.citationActa Crystallographica Section F: Structural Biology And Crystallization Communications, 2008, v. 64 n. 7, p. 602-604en_US
dc.identifier.issn1744-3091en_US
dc.identifier.urihttp://hdl.handle.net/10722/171768-
dc.description.abstractHuman small glutamine-rich tetratricopeptide-repeat protein (hSGT) is a 35 kDa protein implicated in a number of biological processes that include apoptosis, cell division and intracellular cell transport. The tetratricopeptide-repeat (TPR) domain of hSGT has been cloned and expressed in Escherichia coli and purified. Here, the crystallization and preliminary diffraction analysis of the TPR domain of hSGT is reported. X-ray diffraction data were processed to a resolution of 2.4 Å. Crystals belong to space group P21212, with unit-cell parameters a = 67.82, b = 81.93, c = 55.92 Å, α = β = γ = 90°. © International Union of Crystallography 2008.en_US
dc.languageengen_US
dc.publisherWiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www3.interscience.wiley.com/journal/117982340/homeen_US
dc.relation.ispartofActa Crystallographica Section F: Structural Biology and Crystallization Communicationsen_US
dc.subject.meshCarrier Proteins - Biosynthesis - Genetics - Isolation & Purificationen_US
dc.subject.meshCrystallography, X-Rayen_US
dc.subject.meshHumansen_US
dc.subject.meshProtein Structure, Tertiary - Geneticsen_US
dc.subject.meshRecombinant Proteins - Biosynthesis - Genetics - Isolation & Purificationen_US
dc.subject.meshRepetitive Sequences, Amino Acid - Geneticsen_US
dc.subject.meshTandem Repeat Sequences - Geneticsen_US
dc.subject.meshViral Regulatory And Accessory Proteins - Biosynthesis - Genetics - Isolation & Purificationen_US
dc.titleExpression, purification and preliminary crystallographic analysis of recombinant human small glutamine-rich tetratricopeptide-repeat proteinen_US
dc.typeArticleen_US
dc.identifier.emailKotaka, M:masayo@hku.hken_US
dc.identifier.authorityKotaka, M=rp00293en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1107/S1744309108009299en_US
dc.identifier.pmid18607086-
dc.identifier.scopuseid_2-s2.0-46949104113en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-46949104113&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume64en_US
dc.identifier.issue7en_US
dc.identifier.spage602en_US
dc.identifier.epage604en_US
dc.identifier.isiWOS:000257249000008-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridDutta, S=24464182000en_US
dc.identifier.scopusauthoridKotaka, M=6604073578en_US
dc.identifier.scopusauthoridTan, YJ=7402139791en_US
dc.identifier.citeulike2885219-

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