GSBS Student Publications

Title

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

Publication Date

1998-10-17

UMMS Affiliation

Graduate School of Biomedical Sciences; Program in Molecular Medicine; Department of Cell Biology

Document Type

Article

Disciplines

Life Sciences | Medicine and Health Sciences

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.

DOI of Published Version

10.1006/jsbi.1998.4016

Source

J Struct Biol. 1998 Sep;123(1):83-5. Link to article on publisher's site

Journal/Book/Conference Title

Journal of structural biology

Related Resources

Link to Article in PubMed

PubMed ID

9774548

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