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- Publisher Website: 10.1107/S1744309108009299
- Scopus: eid_2-s2.0-46949104113
- PMID: 18607086
- WOS: WOS:000257249000008
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Article: Expression, purification and preliminary crystallographic analysis of recombinant human small glutamine-rich tetratricopeptide-repeat protein
Title | Expression, purification and preliminary crystallographic analysis of recombinant human small glutamine-rich tetratricopeptide-repeat protein |
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Authors | |
Keywords | Human immunodeficiency virus type 1 Small glutamine-rich tetratricopeptide repeat protein Tetratricopeptide repeat |
Issue Date | 2008 |
Publisher | Wiley-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? |
Abstract | Human 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 Identifier | http://hdl.handle.net/10722/171768 |
ISSN | 2014 Impact Factor: 0.524 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
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dc.contributor.author | Dutta, S | en_US |
dc.contributor.author | Kotaka, M | en_US |
dc.contributor.author | Tan, YJ | en_US |
dc.date.accessioned | 2012-10-30T06:16:55Z | - |
dc.date.available | 2012-10-30T06:16:55Z | - |
dc.date.issued | 2008 | en_US |
dc.identifier.citation | Acta Crystallographica Section F: Structural Biology And Crystallization Communications, 2008, v. 64 n. 7, p. 602-604 | en_US |
dc.identifier.issn | 1744-3091 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/171768 | - |
dc.description.abstract | Human 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.language | eng | en_US |
dc.publisher | Wiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www3.interscience.wiley.com/journal/117982340/home | en_US |
dc.relation.ispartof | Acta Crystallographica Section F: Structural Biology and Crystallization Communications | en_US |
dc.subject | Human immunodeficiency virus type 1 | - |
dc.subject | Small glutamine-rich tetratricopeptide repeat protein | - |
dc.subject | Tetratricopeptide repeat | - |
dc.subject.mesh | Carrier Proteins - Biosynthesis - Genetics - Isolation & Purification | en_US |
dc.subject.mesh | Crystallography, X-Ray | en_US |
dc.subject.mesh | Humans | en_US |
dc.subject.mesh | Protein Structure, Tertiary - Genetics | en_US |
dc.subject.mesh | Recombinant Proteins - Biosynthesis - Genetics - Isolation & Purification | en_US |
dc.subject.mesh | Repetitive Sequences, Amino Acid - Genetics | en_US |
dc.subject.mesh | Tandem Repeat Sequences - Genetics | en_US |
dc.subject.mesh | Viral Regulatory And Accessory Proteins - Biosynthesis - Genetics - Isolation & Purification | en_US |
dc.title | Expression, purification and preliminary crystallographic analysis of recombinant human small glutamine-rich tetratricopeptide-repeat protein | en_US |
dc.type | Article | en_US |
dc.identifier.email | Kotaka, M:masayo@hku.hk | en_US |
dc.identifier.authority | Kotaka, M=rp00293 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1107/S1744309108009299 | en_US |
dc.identifier.pmid | 18607086 | - |
dc.identifier.scopus | eid_2-s2.0-46949104113 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-46949104113&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 64 | en_US |
dc.identifier.issue | 7 | en_US |
dc.identifier.spage | 602 | en_US |
dc.identifier.epage | 604 | en_US |
dc.identifier.isi | WOS:000257249000008 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Dutta, S=24464182000 | en_US |
dc.identifier.scopusauthorid | Kotaka, M=6604073578 | en_US |
dc.identifier.scopusauthorid | Tan, YJ=7402139791 | en_US |
dc.identifier.citeulike | 2885219 | - |
dc.identifier.issnl | 1744-3091 | - |