Crystallization and preliminary X-ray diffraction analysis of L-aminoacylase from the hyperthermophilic archaeon Thermococcus litoralis

Rhombohedral crystals of L-aminoacylase from T. litoralis have been grown by the sitting-drop vapour-diffusion technique from recombinant protein expressed in E. coli. The crystals show diffraction to 2.8 Å resolution. The position of the zinc ion has been located using the anomalous data.