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:
-
- Gene Regulation Laboratory, National Institute of Immunology, New Delhi 110067 (India)
- European Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstrasse 1, 69117 Heidelberg (Germany)
- 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}
}