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Title: Crystallization of the C-terminal domain of the mouse brain cytosolic long-chain acyl-CoA thioesterase

Abstract

The C-terminal domain of the mouse long-chain acyl-CoA thioesterase has been expressed in bacteria and crystallized by vapour diffusion. The crystals diffract to 2.4 Å resolution. The mammalian long-chain acyl-CoA thioesterase, the enzyme that catalyses the hydrolysis of acyl-CoAs to free fatty acids, contains two fused 4HBT (4-hydroxybenzoyl-CoA thioesterase) motifs. The C-terminal domain of the mouse long-chain acyl-CoA thioesterase (Acot7) has been expressed in bacteria and crystallized. The crystals were obtained by vapour diffusion using PEG 2000 MME as precipitant at pH 7.0 and 290 K. The crystals have the symmetry of space group R32 (unit-cell parameters a = b = 136.83, c = 99.82 Å, γ = 120°). Two molecules are expected in the asymmetric unit. The crystals diffract to 2.4 Å resolution using the laboratory X-ray source and are suitable for crystal structure determination.

Authors:
;  [1];  [1];  [2];  [2];  [2]; ;  [1];  [2];  [2]
  1. School of Molecular and Microbial Sciences, University of Queensland, Brisbane, Queensland 4072 (Australia)
  2. (Australia)
Publication Date:
OSTI Identifier:
22356271
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 62; Journal Issue: Pt 2; Other Information: PMCID: PMC2150959; PMID: 16511283; PUBLISHER-ID: pu5122; OAI: oai:pubmedcentral.nih.gov:2150959; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CARBOXYLIC ACIDS; CRYSTAL STRUCTURE; CRYSTALLIZATION; CRYSTALS; DIFFUSION; MOLECULES; RESOLUTION; SPACE GROUPS; SYMMETRY; X-RAY SOURCES

Citation Formats

Serek, Robert, Forwood, Jade K., Hume, David A., Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Cooperative Research Centre for Chronic Inflammatory Diseases, University of Queensland, Brisbane, Queensland 4072, Special Research Centre for Functional and Applied Genomics, University of Queensland, Brisbane, Queensland 4072, Martin, Jennifer L., Kobe, Bostjan, E-mail: b.kobe@uq.edu.au, Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, and Special Research Centre for Functional and Applied Genomics, University of Queensland, Brisbane, Queensland 4072. Crystallization of the C-terminal domain of the mouse brain cytosolic long-chain acyl-CoA thioesterase. United Kingdom: N. p., 2006. Web. doi:10.1107/S1744309106000030.
Serek, Robert, Forwood, Jade K., Hume, David A., Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Cooperative Research Centre for Chronic Inflammatory Diseases, University of Queensland, Brisbane, Queensland 4072, Special Research Centre for Functional and Applied Genomics, University of Queensland, Brisbane, Queensland 4072, Martin, Jennifer L., Kobe, Bostjan, E-mail: b.kobe@uq.edu.au, Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, & Special Research Centre for Functional and Applied Genomics, University of Queensland, Brisbane, Queensland 4072. Crystallization of the C-terminal domain of the mouse brain cytosolic long-chain acyl-CoA thioesterase. United Kingdom. doi:10.1107/S1744309106000030.
Serek, Robert, Forwood, Jade K., Hume, David A., Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Cooperative Research Centre for Chronic Inflammatory Diseases, University of Queensland, Brisbane, Queensland 4072, Special Research Centre for Functional and Applied Genomics, University of Queensland, Brisbane, Queensland 4072, Martin, Jennifer L., Kobe, Bostjan, E-mail: b.kobe@uq.edu.au, Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, and Special Research Centre for Functional and Applied Genomics, University of Queensland, Brisbane, Queensland 4072. Wed . "Crystallization of the C-terminal domain of the mouse brain cytosolic long-chain acyl-CoA thioesterase". United Kingdom. doi:10.1107/S1744309106000030.
@article{osti_22356271,
title = {Crystallization of the C-terminal domain of the mouse brain cytosolic long-chain acyl-CoA thioesterase},
author = {Serek, Robert and Forwood, Jade K. and Hume, David A. and Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072 and Cooperative Research Centre for Chronic Inflammatory Diseases, University of Queensland, Brisbane, Queensland 4072 and Special Research Centre for Functional and Applied Genomics, University of Queensland, Brisbane, Queensland 4072 and Martin, Jennifer L. and Kobe, Bostjan, E-mail: b.kobe@uq.edu.au and Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072 and Special Research Centre for Functional and Applied Genomics, University of Queensland, Brisbane, Queensland 4072},
abstractNote = {The C-terminal domain of the mouse long-chain acyl-CoA thioesterase has been expressed in bacteria and crystallized by vapour diffusion. The crystals diffract to 2.4 Å resolution. The mammalian long-chain acyl-CoA thioesterase, the enzyme that catalyses the hydrolysis of acyl-CoAs to free fatty acids, contains two fused 4HBT (4-hydroxybenzoyl-CoA thioesterase) motifs. The C-terminal domain of the mouse long-chain acyl-CoA thioesterase (Acot7) has been expressed in bacteria and crystallized. The crystals were obtained by vapour diffusion using PEG 2000 MME as precipitant at pH 7.0 and 290 K. The crystals have the symmetry of space group R32 (unit-cell parameters a = b = 136.83, c = 99.82 Å, γ = 120°). Two molecules are expected in the asymmetric unit. The crystals diffract to 2.4 Å resolution using the laboratory X-ray source and are suitable for crystal structure determination.},
doi = {10.1107/S1744309106000030},
journal = {Acta Crystallographica. Section F},
number = Pt 2,
volume = 62,
place = {United Kingdom},
year = {Wed Feb 01 00:00:00 EST 2006},
month = {Wed Feb 01 00:00:00 EST 2006}
}