Overproduction, crystallization and preliminary X-ray crystallographic analysis of Escherichia coli tRNA N6-threonylcarbamoyladenosine dehydratase

Escherichia coli tRNA N6-threonylcarbamoyladenosine dehydratase (TcdA), previously called CsdL or YgdL, was overproduced and purified from E. coli and crystallized using polyethylene glycol 3350 as a crystallizing agent. X-ray diffraction data were collected to 2.70 Å resolution under cryoconditions using synchrotron X-rays. The crystals belonged to space group P21, with unit-cell parameters a = 65.4, b = 96.8, c = 83.3 Å, β = 111.7°. According to the Matthews coefficient, the asymmetric unit may contain up to four subunits of the monomeric protein, with a crystal volume per protein mass (VM) of 2.12 Å3 Da−1 and 42.1% solvent content.

Source: Acta Crystallographica Section F - October 25, 2014 Category: Biochemistry Authors: Kim, S.Kim, K.Y.Park, J.K.Lee, B.I.Kim, Y.-G.Park, S. Tags: tRNA hypermodification N6-threonylcarbamoyladenosine dehydratase TcdA CsdL crystallization communications Source Type: research