The tRNA-specific adenosine deaminase from the pathogenic bacteria Streptococcus pyogenes (spTAD) has been overexpressed in Escherichia coli and crystallized in the presence of Zn2+ ion at 295 K using ammonium sulfate as a precipitant. Flash-cooled crystals of spTAD diffracted to 2.0 Å using 30%(v/v) glycerol as a cryoprotectant. X-ray diffraction data have been collected to 2.0 Å using synchrotron radiation. The crystal belongs to the tetragonal space group P42212, with unit-cell parameters a = b = 81.042, c = 81.270 Å. The asymmetric unit contains one subunit of spTAD, with a corresponding crystal volume per protein weight (V M) of 3.3 Å3 Da-1 and a solvent content of 62.7%.
|Number of pages||3|
|Journal||Acta Crystallographica Section F: Structural Biology and Crystallization Communications|
|Publication status||Published - 2005 Dec 1|
ASJC Scopus subject areas
- Structural Biology
- Condensed Matter Physics