Crystallization and preliminary X-ray crystallographic analysis of the GluR0 ligand-binding core from Nostoc punctiforme

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Nov 1;61(Pt 11):1020-2. doi: 10.1107/S1744309105034329. Epub 2005 Oct 28.

Abstract

GluR0 from Nostoc punctiforme (NpGluR0) is a bacterial homologue of the ionotropic glutamate receptor. The ligand-binding core of NpGluR0 was crystallized at 294 K using the hanging-drop vapour-diffusion method. The L-glutamate-complexed crystal belongs to space group C222(1), with unit-cell parameters a = 78.0, b = 145.1, c = 132.1 A. The crystals contain three subunits in the asymmetric unit, with a VM value of 2.49 A3 Da(-1). The diffraction limit of the L-glutamate complex data set was 2.1 A using synchrotron X-ray radiation at beamline BL-4A of the Pohang Accelerator Laboratory (Pohang, Korea).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cryopreservation
  • Crystallization
  • Crystallography, X-Ray
  • Diffusion
  • Glutamic Acid / chemistry
  • Ligands
  • Molecular Sequence Data
  • Nostoc / metabolism*
  • Protein Binding
  • Protein Conformation
  • Receptors, Glutamate / chemistry*
  • Sequence Homology, Amino Acid
  • Synchrotrons
  • Temperature
  • X-Ray Diffraction

Substances

  • Ligands
  • Receptors, Glutamate
  • Glutamic Acid