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

As a thermostable esterase with cold adaptation, EstL5 might be of significant industrial interest and value in scientific research. In order to provide new insights into the structure-function relationship of EstL5 and to help better understand the biochemical data, a project to determine the three-dimensional structure of this enzyme was initiated.