Cloning, expression, purification, crystallization and initial crystallographic analysis of transcription elongation factors GreB from Escherichia coli and Gfh1 from Thermus thermophilus

摘要

The GreB transcription cleavage factor of E. coli and the Gfh1 transcription elongation factor of T. thermophilus were cloned, expressed, purified and crystallized. Complete diffraction data sets were collected for the GreB and Gfh1 crystals to 2.6 and 2.8 Å resolution, respectively. Structure determination of these proteins is now in progress.