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Expression, purification, and crystallization of two isozymes of 6- phosphoglucose isomerase of bacillus stearothermophilus
Journal article   Peer reviewed

Expression, purification, and crystallization of two isozymes of 6- phosphoglucose isomerase of bacillus stearothermophilus

Chwan-Deng Hsiao, Chia-Cheng Chou, Yi-Yuong Hsiao, Yuh-Ju Sun and Menghsiao Meng
Journal of Structural Biology, Vol.120(2), pp.196-200
11/1997

Abstract

6-phosphoglucose isomerase Bacillus stearothermophilus Protein crystals
Two isozymes of 6-phosphoglucose isomerase (phosphoglucose isomerase A and phosphoglucose isomerase B), isolated from Bacillus stearothermophilus, have been overexpressed in Escherichia coli strain DF2145 and purified to homogeneity. Crystals of both isozymes have been obtained by the vapor diffusion method. The crystals of phosphoglucose isomerase A have unit cell dimensions a = b = 132.0 Å c = 183.6 Å and diffract to about 2.8 Å resolution. An analysis of the reflection data indicates that the crystal system is hexagonal, space group P6 1 22 or P6 5 22. The crystals of phosphoglucose isomerase B complexed with 6-phosphogluconate belong to the orthorhombic space group I222 (or I2 1 2 1 2 1 ), with cell dimensions a = 75.1 Å b = 95.7 Å, c = 171.5 Å and diffract to a resolution of 2.3 Å. These crystals promise to yield more detail for the substrate recognition and higher resolution structures of 6-phosphoglucose isomerase.

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