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

UMMS Affiliation

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

Date

10-17-1998

Document Type

Article

Medical Subject Headings

Animals; *Crystallization; Crystallography, X-Ray; Glutathione Transferase; Nuclear Proteins; Polyethylene Glycols; Protein Sorting Signals; Recombinant Fusion Proteins; Schistosoma; Transcription Factors

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.

Rights and Permissions

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

DOI of Published Version

10.1006/jsbi.1998.4016

Related Resources

Link to Article in PubMed

Journal Title

Journal of structural biology

PubMed ID

9774548