Preliminary crystallographic study of glutathione S-transferase fused with the nuclear matrix targeting signal of the transcription factor AML- 1/CBF-α2

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

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

A glutathione S-transferase fused with the nuclear matrix targeting signal (GST-NMTS) of AML-1/CBF-α2 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-α2 protein to the nuclear matrix. The crystal belongs to tetragonal space group P43212 with unit cell dimensions a = b = 93.4 Å, c = 57.6 Å. There is one GST- fusion protein per asymmetric unit. Crystals diffracted to at least 2.7 Å and are appropriate for structure determination.

Original languageEnglish (US)
Pages (from-to)83-85
Number of pages3
JournalJournal of Structural Biology
Volume123
Issue number1
DOIs
StatePublished - Sep 1998

Keywords

  • Leukemia
  • Nuclear matrix
  • X-ray diffraction

ASJC Scopus subject areas

  • Structural Biology

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