title: Crystallization and preliminary X-ray characterization of aminopeptidase N from Escherichia coli.
abstract: A recombinant form of aminopeptidase N (molecular weight 99 kDa) from Escherichia coli was crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitating agent. The crystals belong to the hexagonal space group P3(1)21, with unit-cell parameters a = b = 120.5, c = 171.0 angstroms. The crystals are most likely to contain one molecule in the asymmetric unit, with a V(M) value of 3.62 angstroms3 Da(-1). Diffraction data were collected to 2.0 angstroms resolution using Cu Kalpha radiation from a rotating-anode X-ray generator.
authors.affiliation: Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan.
authors.forename: Yuko
authors.initials: Y
authors.lastname: Onohara
authors.forename: Yoshitaka
authors.initials: Y
authors.lastname: Nakajima
authors.forename: Kiyoshi
authors.initials: K
authors.lastname: Ito
authors.forename: Yue
authors.initials: Y
authors.lastname: Xu
authors.forename: Kanako
authors.initials: K
authors.lastname: Nakashima
authors.forename: Takashi
authors.initials: T
authors.lastname: Ito
authors.forename: Tadashi
authors.initials: T
authors.lastname: Yoshimoto
mesh_terms: D018826:CD13 Antigens / Q000737:chemistry* / Q000302:isolation & purification*; D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D014961:X-Ray Diffraction
chemical_list: D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; D018826:CD13 Antigens