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Preliminary crystallographic study of glutathione S-transferase fused with the nuclear matrix targeting signal of the transcription factor AML-1/CBF-alpha2

dc.contributor.authorTang, Lei
dc.contributor.authorGuo, Bo
dc.contributor.authorVan Wijnen, Andre J.
dc.contributor.authorLian, Jane B.
dc.contributor.authorStein, Janet L.
dc.contributor.authorStein, Gary S.
dc.contributor.authorZhou, G. Wayne
dc.date2022-08-11T08:08:49.000
dc.date.accessioned2022-08-23T16:09:20Z
dc.date.available2022-08-23T16:09:20Z
dc.date.issued1998-10-17
dc.date.submitted2009-01-13
dc.identifier.citationJ Struct Biol. 1998 Sep;123(1):83-5. <a href="http://dx.doi.org/10.1006/jsbi.1998.4016">Link to article on publisher's site</a>
dc.identifier.issn1047-8477 (Print)
dc.identifier.doi10.1006/jsbi.1998.4016
dc.identifier.pmid9774548
dc.identifier.urihttp://hdl.handle.net/20.500.14038/32669
dc.description.abstractA glutathione S-transferase fused with the nuclear matrix targeting signal (GST-NMTS) of AML-1/CBF-alpha2 has been crystallized by the vapor diffusion method using polyethylene glycol (PEG) as the precipitant. The NMTS is a 31-amino-acid signal peptide that can target the AML-1/CBF-alpha2 protein to the nuclear matrix. The crystal belongs to tetragonal space group P43212 with unit cell dimensions a = b = 93.4 A, c = 57.6 A. There is one GST-fusion protein per asymmetric unit. Crystals diffracted to at least 2.7 A and are appropriate for structure determination.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=9774548&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1006/jsbi.1998.4016
dc.subjectAnimals; *Crystallization; Crystallography, X-Ray; Glutathione Transferase; Nuclear Proteins; Polyethylene Glycols; Protein Sorting Signals; Recombinant Fusion Proteins; Schistosoma; Transcription Factors
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titlePreliminary crystallographic study of glutathione S-transferase fused with the nuclear matrix targeting signal of the transcription factor AML-1/CBF-alpha2
dc.typeJournal Article
dc.source.journaltitleJournal of structural biology
dc.source.volume123
dc.source.issue1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/1229
dc.identifier.contextkey693139
html.description.abstract<p>A glutathione S-transferase fused with the nuclear matrix targeting signal (GST-NMTS) of AML-1/CBF-alpha2 has been crystallized by the vapor diffusion method using polyethylene glycol (PEG) as the precipitant. The NMTS is a 31-amino-acid signal peptide that can target the AML-1/CBF-alpha2 protein to the nuclear matrix. The crystal belongs to tetragonal space group P43212 with unit cell dimensions a = b = 93.4 A, c = 57.6 A. There is one GST-fusion protein per asymmetric unit. Crystals diffracted to at least 2.7 A and are appropriate for structure determination.</p>
dc.identifier.submissionpathgsbs_sp/1229
dc.contributor.departmentDepartment of Cell Biology
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages83-5


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