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 = ...

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Detalles Bibliográficos
Autores principales: Onohara, Yuko, Nakajima, Yoshitaka, Ito, Kiyoshi, Xu, Yue, Nakashima, Kanako, Ito, Takashi, Yoshimoto, Tadashi
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2006
Materias:
Crystallization Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2242940/
https://www.ncbi.nlm.nih.gov/pubmed/16820698
http://dx.doi.org/10.1107/S1744309106021567
Descripción
Sumario: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 Å. The crystals are most likely to contain one molecule in the asymmetric unit, with a V (M) value of 3.62 Å(3) 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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