Open AccessPurification, crystallization and preliminary X‐ray crystallographic analysis of the outer membrane lipoprotein NlpE from Escherichia coli
Author(s) -
Hirano Yu,
Hossain Md. Motarab,
Takeda Kazuki,
Tokuda Hajime,
Miki Kunio
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106045313
Subject(s) - crystallization , escherichia coli , bacterial outer membrane , crystallography , x ray , materials science , chemistry , membrane , biochemistry , physics , gene , optics , organic chemistry
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 Å resolution and belong to space group P 4 3 2 1 2. The monoclinic crystals diffracted to 3.0 Å resolution and belong to space group C 2. Initial phases were obtained from a tetragonal crystal of selenomethionylated protein by the MAD method.