Preliminary crystallographic study of glutathione S-transferase fused with the nuclear matrix targeting signal of the transcription factor AML-1/CBF-alpha2
Van Wijnen, Andre J.
Lian, Jane B.
Stein, Janet L.
Stein, Gary S.
Zhou, G. Wayne
UMass Chan AffiliationsDepartment of Cell Biology
Program in Molecular Medicine
Graduate School of Biomedical Sciences
KeywordsAnimals; *Crystallization; Crystallography, X-Ray; Glutathione Transferase; Nuclear Proteins; Polyethylene Glycols; Protein Sorting Signals; Recombinant Fusion Proteins; Schistosoma; Transcription Factors
Medicine and Health Sciences
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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.
SourceJ Struct Biol. 1998 Sep;123(1):83-5. Link to article on publisher's site
Permanent Link to this Itemhttp://hdl.handle.net/20.500.14038/32669
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