Crystallization and preliminary X-ray diffraction analysis of a thermostable GDSL-family esterase, EstL5, from Geobacillus thermodenitrificans T2.

The novel thermostable esterase EstL5 belonging to the GDSL family exhibits a unique cold-adaptation feature at low temperatures. To better understand its biochemical and enzymatic properties, recombinant EstL5 protein was purified and crystallized using the vapour-diffusion method. The EstL5 crystals diffracted X-rays to 2.79 Ã resolution using a synchrotron-radiation source, belonged to the tetragonal space group P41212 or P43212, with unit-cell parameters a = b = 101.51, c = 124.22 Ã , and are expected to contain two molecules in each asymmetric unit. To obtain initial phases, selenomethionyl-substituted protein was overproduced. Purified SeMet-labelled EstL5 protein was crystallized and formed crystals that diffracted to a resolution of 3.0 Ã .