title: Purification, crystallization and preliminary X-ray crystallographic analysis of the outer membrane lipoprotein NlpE from Escherichia coli.
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.
authors.affiliation: Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
authors.forename: Yu
authors.initials: Y
authors.lastname: Hirano
authors.forename: Md Motarab
authors.initials: MM
authors.lastname: Hossain
authors.forename: Kazuki
authors.initials: K
authors.lastname: Takeda
authors.forename: Hajime
authors.initials: H
authors.lastname: Tokuda
authors.forename: Kunio
authors.initials: K
authors.lastname: Miki
mesh_terms: D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000302:isolation & purification; D008074:Lipoproteins / Q000737:chemistry* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D016415:Sequence Alignment
chemical_list: D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; D008074:Lipoproteins; C095021:NlpE protein, E coli