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Title: Expression, purification, crystallization and preliminary X-ray analysis of the ligand-binding domain of metabotropic glutamate receptor 7

Abstract

The ligand-binding domain of metabotropic glutamate receptor 7 has been overexpressed, purified, and crystallized by the hanging-drop vapour-diffusion method. A complete data set has been collected to 3.30 Å. Glutamate is the major excitatory neurotransmitter and its metabotropic glutamate receptor (mGluR) plays an important role in the central nervous system. The ligand-binding domain (LBD) of mGluR subtype 7 (mGluR7) was produced using the baculovirus expression system and purified from the culture medium. The purified protein was characterized by gel-filtration chromatography, SDS–PAGE and a ligand-binding assay. Crystals of mGluR7 LBD were grown at 293 K by the hanging-drop vapour-diffusion method. The crystals diffracted X-rays to 3.30 Å resolution using synchrotron radiation and belong to the trigonal space group P3{sub 1}21, with unit-cell parameters a = b = 92.4, c = 114.3 Å. Assuming the presence of one protomer per crystallographic asymmetric unit, the Matthews coefficient V{sub M} was calculated to be 2.5 Å{sup 3} Da{sup −1} and the solvent content was 51%.

Authors:
; ; ;  [1]
  1. Biomolecular Engineering Research Institute, Suita, Osaka 565-0874 (Japan)
Publication Date:
OSTI Identifier:
22360374
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 63; Journal Issue: Pt 7; Other Information: PMCID: PMC2335145; PMID: 17620729; PUBLISHER-ID: ll5120; OAI: oai:pubmedcentral.nih.gov:2335145; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; DIFFUSION; GELS; LIGANDS; RECEPTORS; RESOLUTION; SOLVENTS; SPACE GROUPS; SYNCHROTRON RADIATION

Citation Formats

Muto, Takanori, Tsuchiya, Daisuke, Morikawa, Kosuke, and Jingami, Hisato. Expression, purification, crystallization and preliminary X-ray analysis of the ligand-binding domain of metabotropic glutamate receptor 7. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107030059.
Muto, Takanori, Tsuchiya, Daisuke, Morikawa, Kosuke, & Jingami, Hisato. Expression, purification, crystallization and preliminary X-ray analysis of the ligand-binding domain of metabotropic glutamate receptor 7. United Kingdom. https://doi.org/10.1107/S1744309107030059
Muto, Takanori, Tsuchiya, Daisuke, Morikawa, Kosuke, and Jingami, Hisato. 2007. "Expression, purification, crystallization and preliminary X-ray analysis of the ligand-binding domain of metabotropic glutamate receptor 7". United Kingdom. https://doi.org/10.1107/S1744309107030059.
@article{osti_22360374,
title = {Expression, purification, crystallization and preliminary X-ray analysis of the ligand-binding domain of metabotropic glutamate receptor 7},
author = {Muto, Takanori and Tsuchiya, Daisuke and Morikawa, Kosuke and Jingami, Hisato},
abstractNote = {The ligand-binding domain of metabotropic glutamate receptor 7 has been overexpressed, purified, and crystallized by the hanging-drop vapour-diffusion method. A complete data set has been collected to 3.30 Å. Glutamate is the major excitatory neurotransmitter and its metabotropic glutamate receptor (mGluR) plays an important role in the central nervous system. The ligand-binding domain (LBD) of mGluR subtype 7 (mGluR7) was produced using the baculovirus expression system and purified from the culture medium. The purified protein was characterized by gel-filtration chromatography, SDS–PAGE and a ligand-binding assay. Crystals of mGluR7 LBD were grown at 293 K by the hanging-drop vapour-diffusion method. The crystals diffracted X-rays to 3.30 Å resolution using synchrotron radiation and belong to the trigonal space group P3{sub 1}21, with unit-cell parameters a = b = 92.4, c = 114.3 Å. Assuming the presence of one protomer per crystallographic asymmetric unit, the Matthews coefficient V{sub M} was calculated to be 2.5 Å{sup 3} Da{sup −1} and the solvent content was 51%.},
doi = {10.1107/S1744309107030059},
url = {https://www.osti.gov/biblio/22360374}, journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 7,
volume = 63,
place = {United Kingdom},
year = {Sun Jul 01 00:00:00 EDT 2007},
month = {Sun Jul 01 00:00:00 EDT 2007}
}