Crystal Structure of Human Aspartyl Aminopeptidase (DNPEP) in complex with Aspartic acid Hydroxamate

Structure of human aspartyl aminopeptidase complexed with substrate analogue: insight into catalytic mechanism, substrate specificity and M18 peptidase family.

15% PEG3350, 0.25 M magnesium chloride, 0.1 M Tris, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K

RESIDUES -9 THROUGH 0 ARE A NATURAL EXPRESSION TAG (AS PER UNP Q53SB6).

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED

Structural Genomics, Structural Genomics Consortium, SGC, HYDROLASE