X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica

MPPITQQATVTAWLPQVDASQITGTISSLESFTNRFYTTTSGAQASDWIASEWQALSASLPNASVKQVSHSGYNQKSVVM
TITGSEAPDEWIVIGGHLDSTIGSHTNEQSVAPGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAEEVGLRGSQD
LANQYKSEGKNVVSALQLDMTNYKGSAQDVVFITDYTDSNFTQYLTQLMDEYLPSLTYGFDTCGYACSDHASWHNAGYPA
AMPFESKFNDYNPRIHTTQDTLANSDPTGSHAKKFTQLGLAYAIEMGSATG

100 mM Tris pH 8.0, 100 mM KSCN, 4.5 M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 298KK

AAP with Tris bound at high resolution (1.2 A)

monomeric enzyme. The monomer comprises the ASU

Tris, peptidase, aminohydrolase, Cobalt, metalloprotease, HYDROLASE