Download MendeleyPreliminary crystallographic study of glutathione S-transferase fused with the nuclear matrix targeting signal of the transcription factor AML-1/CBF-alpha2.
Tang, L., Guo, B., van Wijnen, A.J., Lian, J.B., Stein, J.L., Stein, G.S., Zhou, G.W.(1998) J Struct Biol 123: 83-85
- PubMed: 9774548
- DOI: https://doi.org/10.1006/jsbi.1998.4016
- Primary Citation of Related Structures:
1B8X - PubMed 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.
Organizational Affiliation:
Program in Molecular Medicine, UMASS Medical Center, Worcester, Massachusetts, 01605, USA.
