Open AccessCrystallization and preliminary X‐ray crystallographic analysis of the GluR0 ligand‐binding core from Nostoc punctiforme
Author(s) -
Lee Jun Hyuck,
Im Young Jun,
Park Soo Jeong,
Rho SeongHwan,
Kim MunKyoung,
Kang Gil Bu,
Eom Soo Hyun
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105034329
Subject(s) - crystallography , ligand (biochemistry) , crystallization , beamline , synchrotron radiation , resolution (logic) , monomer , materials science , chemistry , physics , receptor , optics , polymer , biochemistry , organic chemistry , artificial intelligence , computer science , composite material , beam (structure)
GluR0 from Nostoc punctiforme ( Np GluR0) is a bacterial homologue of the ionotropic glutamate receptor. The ligand‐binding core of Np GluR0 was crystallized at 294 K using the hanging‐drop vapour‐diffusion method. The l ‐glutamate‐complexed crystal belongs to space group C 222 1 , with unit‐cell parameters a = 78.0, b = 145.1, c = 132.1 Å. The crystals contain three subunits in the asymmetric unit, with a V M value of 2.49 Å 3 Da −1 . The diffraction limit of the l ‐glutamate complex data set was 2.1 Å using synchrotron X‐ray radiation at beamline BL‐4A of the Pohang Accelerator Laboratory (Pohang, Korea).