Abstract
Aminopeptidases (APs) are a group of exopeptidases that catalyze the removal of amino acids from the N-termini of proteins and peptides. The APs are ubiquitous in nature and are of critical biological and medical importance because of their key role in protein degradation. Pseudomonas aeruginosa aspartyl aminopeptidase (PaAAP), which is encoded by the apeB gene, was expressed in Escherichia coli, purified and crystallized using the microbatch method. A preliminary structural study has been performed using the X-ray crystallographic method. The PaAAP crystal diffracted to 2.0 Å resolution and belonged to the rhombohedral space group H3, with unit-cell parameters a = b = 133.6, c = 321.2. The unit-cell volume of the crystal is compatible with the presence of four monomers in the asymmetric unit, with a corresponding Matthews coefficient V(M) of 2.95 Å(3) Da(-1) and a solvent content of 58.3%.