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

J Struct Biol. 1998 Sep;123(1):83-5. doi: 10.1006/jsbi.1998.4016.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

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

Substances

  • Nuclear Proteins
  • Protein Sorting Signals
  • Recombinant Fusion Proteins
  • Transcription Factors
  • Polyethylene Glycols
  • Glutathione Transferase