Crystallization and preliminary X-ray characterization of aminopeptidase N from Escherichia coli
Crystallization and preliminary X-ray characterization of aminopeptidase N from Escherichia coli
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DOI：
10.1107/s1744309106021567
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发表时间：
2006-07-01
影响因子：
0.9
通讯作者：
Yoshimoto, Tadashi
中科院分区：
文献类型：
--
作者：
Onohara, Yuko;Nakajima, Yoshitaka;Yoshimoto, Tadashi
用硫酸铵作沉淀剂，通过悬滴气相扩散法从大肠杆菌中结晶出重组形式的氨肽酶N（分子量99 kDa）。晶体属于六方晶系空间群P3（1）21，晶胞参数a = B = 120.5，c = 171.0埃。晶体中最有可能在不对称单元中包含一个分子，V-M值为3.62埃（3）Da（-1）。使用来自双阳极X射线发生器的Cu K α辐射收集衍射数据至2.0埃分辨率。
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 angstrom. The crystals are most likely to contain one molecule in the asymmetric unit, with a V-M value of 3.62 angstrom(3) Da(-1). Diffraction data were collected to 2.0 angstrom resolution using Cu K alpha radiation from a rotating-anode X-ray generator.