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Crystallization and preliminary X‐ray characterization of aminopeptidase N from Escherichia coli

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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 P3121, with unit‐cell parameters a = b = 120.5, c = 171.0 Å. The crystals are most likely to contain one molecule in the asymmetric unit, with a V M value of 3.62 Å3 Da−1. Diffraction data were collected to 2.0 Å resolution using Cu Kα radiation from a rotating‐anode X‐ray generator.
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Keywords: aminopeptidase N

Document Type: Research Article

Affiliations: Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8521, Japan

Publication date: July 1, 2006

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