Premium
Crystallization and preliminary X‐ray diffraction analysis of the periplasmic domain of the Escherichia coli aspartate receptor Tar and its complex with aspartate
Author(s) -
Mise Takeshi,
Matsunami Hideyuki,
Samatey Fadel A.,
Maruyama Ichiro N.
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14014733
Subject(s) - periplasmic space , escherichia coli , crystallization , ammonium sulfate , crystallography , chemistry , operon , nuclear chemistry , stereochemistry , biochemistry , chromatography , organic chemistry , gene
The cell‐surface receptor Tar mediates bacterial chemotaxis toward an attractant, aspartate (Asp), and away from a repellent, Ni 2+ . To understand the molecular mechanisms underlying the induction of Tar activity by its ligands, the Escherichia coli Tar periplasmic domain with and without bound aspartate (Asp‐Tar and apo‐Tar, respectively) were each crystallized in two different forms. Using ammonium sulfate as a precipitant, crystals of apo‐Tar1 and Asp‐Tar1 were grown and diffracted to resolutions of 2.10 and 2.40 Å, respectively. Alternatively, using sodium chloride as a precipitant, crystals of apo‐Tar2 and Asp‐Tar2 were grown and diffracted to resolutions of 1.95 and 1.58 Å, respectively. Crystals of apo‐Tar1 and Asp‐Tar1 adopted space group P 4 1 2 1 2, while those of apo‐Tar2 and Asp‐Tar2 adopted space groups P 2 1 2 1 2 1 and C 2, respectively.