Crystallization and preliminary X-ray characterization of aminopeptidase N from Escherichia coli.
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.
Onohara
Yuko
Y
Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan.
Nakajima
Yoshitaka
Y
Ito
Kiyoshi
K
Xu
Yue
Y
Nakashima
Kanako
K
Ito
Takashi
T
Yoshimoto
Tadashi
T
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
D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; D018826:CD13 Antigens