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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

Tang, Lei
Guo, Bo
Van Wijnen, Andre J.
Lian, Jane B.
Stein, Janet L.
Stein, Gary S.
Zhou, G. Wayne
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Abstract

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 site

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DOI
10.1006/jsbi.1998.4016
PubMed ID
9774548
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