| Literature DB >> 17142903 |
Yu Hirano1, Md Motarab Hossain, Kazuki Takeda, Hajime Tokuda, Kunio Miki.
Abstract
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.Entities:
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Year: 2006 PMID: 17142903 PMCID: PMC2225377 DOI: 10.1107/S1744309106045313
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091