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Title: Crystallization and preliminary X-ray characterization of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv

Abstract

The phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv was crystallized and diffraction data were collected to 2.8 Å resolution. Phosphoglucose isomerase is a ubiquitous enzyme that catalyzes the isomerization of d-glucopyranose-6-phosphate to d-fructofuranose-6-phosphate. The present investigation reports the expression, purification, crystallization and preliminary crystallographic studies of the phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv, which shares 46% sequence identity with that of its human host. The recombinant protein, which was prepared using an Escherichia coli expression system, was crystallized by the hanging-drop vapour-diffusion method. The crystals diffracted to a resolution of 2.8 Å and belonged to the orthorhombic space group I2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 109.0, b = 119.8, c = 138.9 Å.

Authors:
 [1];  [2];  [1]; ;  [3]
  1. Gene Regulation Laboratory, National Institute of Immunology, New Delhi 110067 (India)
  2. European Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg (Germany)
  3. Genes and Proteins Laboratory, National Institute of Immunology, New Delhi 110067 (India)
Publication Date:
OSTI Identifier:
22360312
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 63; Journal Issue: Pt 4; Other Information: PMCID: PMC2330222; PMID: 17401215; PUBLISHER-ID: pu5175; OAI: oai:pubmedcentral.nih.gov:2330222; 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; DIFFRACTION; DIFFUSION; ESCHERICHIA COLI; ISOMERIZATION; PHOSPHATES; RESOLUTION; SPACE GROUPS

Citation Formats

Mathur, Divya, Anand, Kanchan, Mathur, Deepika, Jagadish, Nirmala, Suri, Anil, and Garg, Lalit C., E-mail: lalit@nii.res.in, E-mail: lalitcgarg@yahoo.com. Crystallization and preliminary X-ray characterization of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107013218.
Mathur, Divya, Anand, Kanchan, Mathur, Deepika, Jagadish, Nirmala, Suri, Anil, & Garg, Lalit C., E-mail: lalit@nii.res.in, E-mail: lalitcgarg@yahoo.com. Crystallization and preliminary X-ray characterization of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv. United Kingdom. https://doi.org/10.1107/S1744309107013218
Mathur, Divya, Anand, Kanchan, Mathur, Deepika, Jagadish, Nirmala, Suri, Anil, and Garg, Lalit C., E-mail: lalit@nii.res.in, E-mail: lalitcgarg@yahoo.com. 2007. "Crystallization and preliminary X-ray characterization of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv". United Kingdom. https://doi.org/10.1107/S1744309107013218.
@article{osti_22360312,
title = {Crystallization and preliminary X-ray characterization of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv},
author = {Mathur, Divya and Anand, Kanchan and Mathur, Deepika and Jagadish, Nirmala and Suri, Anil and Garg, Lalit C., E-mail: lalit@nii.res.in, E-mail: lalitcgarg@yahoo.com},
abstractNote = {The phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv was crystallized and diffraction data were collected to 2.8 Å resolution. Phosphoglucose isomerase is a ubiquitous enzyme that catalyzes the isomerization of d-glucopyranose-6-phosphate to d-fructofuranose-6-phosphate. The present investigation reports the expression, purification, crystallization and preliminary crystallographic studies of the phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv, which shares 46% sequence identity with that of its human host. The recombinant protein, which was prepared using an Escherichia coli expression system, was crystallized by the hanging-drop vapour-diffusion method. The crystals diffracted to a resolution of 2.8 Å and belonged to the orthorhombic space group I2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 109.0, b = 119.8, c = 138.9 Å.},
doi = {10.1107/S1744309107013218},
url = {https://www.osti.gov/biblio/22360312}, journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 4,
volume = 63,
place = {United Kingdom},
year = {Sun Apr 01 00:00:00 EDT 2007},
month = {Sun Apr 01 00:00:00 EDT 2007}
}