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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.

SUBMITTER: Onohara Y

PROVIDER: S-EPMC2242940 | biostudies-literature | 2006 Jul

REPOSITORIES: biostudies-literature

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

Onohara Yuko Y Nakajima Yoshitaka Y Ito Kiyoshi K Xu Yue Y Nakashima Kanako K Ito Takashi T Yoshimoto Tadashi T

Acta crystallographica. Section F, Structural biology and crystallization communications 20060626 Pt 7

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 u ...[more]

PMID: 16820698

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