Preliminary crystallographic study of glutathione S-transferase fused with the nuclear matrix targeting signal of the transcription factor AML-1/CBF-alpha2
Authors
Tang, LeiGuo, Bo
Van Wijnen, Andre J.
Lian, Jane B.
Stein, Janet L.
Stein, Gary S.
Zhou, G. Wayne
UMass Chan Affiliations
Department of Cell BiologyProgram in Molecular Medicine
Graduate School of Biomedical Sciences
Document Type
Journal ArticlePublication Date
1998-10-17Keywords
Animals; *Crystallization; Crystallography, X-Ray; Glutathione Transferase; Nuclear Proteins; Polyethylene Glycols; Protein Sorting Signals; Recombinant Fusion Proteins; Schistosoma; Transcription FactorsLife Sciences
Medicine and Health Sciences
Metadata
Show full item recordAbstract
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.Source
J Struct Biol. 1998 Sep;123(1):83-5. Link to article on publisher's siteDOI
10.1006/jsbi.1998.4016Permanent Link to this Item
http://hdl.handle.net/20.500.14038/32669PubMed ID
9774548Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1006/jsbi.1998.4016