Purification, crystallization and preliminary X-ray crystallographic analysis of the outer membrane lipoprotein NlpE from Escherichia coli.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.2006 Dec 01;62(Pt 12):1227-30. Epub 2006 Nov 30
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摘要
The outer membrane lipoprotein NlpE functions in stress response by activating the Cpx signal transduction pathway. The nonlipidated Cys1Ala mutant of NlpE with a C-terminal His tag from Escherichia coli was constructed, overexpressed and purified. Crystals of NlpE were grown in two distinct forms by the sitting-drop vapour-diffusion method at 298 K. The tetragonal crystals diffracted to 2.8 A resolution and belong to space group P4(3)2(1)2. The monoclinic crystals diffracted to 3.0 A resolution and belong to space group C2. Initial phases were obtained from a tetragonal crystal of selenomethionylated protein by the MAD method.
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原始数据
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文献解读
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