Preliminary crystallographic study of glutathione S-transferase fused with the nuclear matrix targeting signal of the transcription factor AML-1/CBF-alpha2.
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.
Program in Molecular Medicine, UMASS Medical Center, Worcester, Massachusetts, 01605, USA.
L
L
Tang
B
B
Guo
A J
AJ
van Wijnen
J B
JB
Lian
J L
JL
Stein
G S
GS
Stein
G W
GW
Zhou
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D005982:Glutathione Transferase / Q000737:chemistry*; D009687:Nuclear Proteins / Q000737:chemistry; D011092:Polyethylene Glycols / Q000378:metabolism; D021382:Protein Sorting Signals / Q000737:chemistry; D011993:Recombinant Fusion Proteins / Q000737:chemistry*; D012547:Schistosoma / Q000737:chemistry*; D014157:Transcription Factors / Q000737:chemistry*
D009687:Nuclear Proteins; D021382:Protein Sorting Signals; D011993:Recombinant Fusion Proteins; D014157:Transcription Factors; D011092:Polyethylene Glycols; D005982:Glutathione Transferase