title: Crystallization and preliminary X-ray studies of human erythrocyte acylpeptide hydrolase.
abstract: Crystals of acylpeptide hydrolase suitable for structure determination have been obtained. This enzyme removes the N-terminal formyl or acetyl group together with the first amino acid residue from N-terminal blocked peptides including bioactive peptides. One set of crystals, which diffract to 2.2 A, are in space group P2 with cell dimensions a = 118.6 A, b = 82.3 A, c = 182.1 A, beta = 91.6 degrees. The search for suitable heavy-atom derivatives is underway.
authors.affiliation: Institute of Molecular Biology, University of Oregon, Eugene 97403.
authors.forename: M
authors.initials: M
authors.lastname: Feese
authors.forename: A
authors.initials: A
authors.lastname: Scaloni
authors.forename: W M
authors.initials: WM
authors.lastname: Jones
authors.forename: J M
authors.initials: JM
authors.lastname: Manning
authors.forename: S J
authors.initials: SJ
authors.lastname: Remington
mesh_terms: D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000737:chemistry*; D003460:Crystallization; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D014961:X-Ray Diffraction
chemical_list: D010447:Peptide Hydrolases; D000626:Aminopeptidases; C038220:acylaminoacyl-peptidase