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

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Title: Crystallization and preliminary X-ray characterization of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv.
Authors: Mathur, Divya1, Anand, Kanchan2, Suri, Anil3, Mathur, Deepika1, Jagadish, Nirmala3, Garg, Lalit C.1 lalit@nii.res.in
Source: Acta Crystallographica: Section F (Wiley-Blackwell). Apr2007, Vol. 63 Issue 4, p353-355. 3p. 1 Color Photograph, 1 Black and White Photograph, 1 Chart.
Subjects: Isomerases, Enzymes, Mycobacterium tuberculosis, Recombinant proteins, Crystallization, Optical diffraction
Abstract: Phosphoglucose isomerase is a ubiquitous enzyme that catalyzes the isomerization ofd-glucopyranose-6-phosphate tod-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 I212121, with unit-cell parameters a = 109.0, b = 119.8, c = 138.9 Å. [ABSTRACT FROM AUTHOR]
Copyright of Acta Crystallographica: Section F (Wiley-Blackwell) is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
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DbLabel: Engineering Source
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  Data: Crystallization and preliminary X-ray characterization of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv.
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  Data: <searchLink fieldCode="JN" term="%22Acta+Crystallographica%3A+Section+F+%28Wiley-Blackwell%29%22">Acta Crystallographica: Section F (Wiley-Blackwell)</searchLink>. Apr2007, Vol. 63 Issue 4, p353-355. 3p. 1 Color Photograph, 1 Black and White Photograph, 1 Chart.
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  Data: <searchLink fieldCode="DE" term="%22Isomerases%22">Isomerases</searchLink><br /><searchLink fieldCode="DE" term="%22Enzymes%22">Enzymes</searchLink><br /><searchLink fieldCode="DE" term="%22Mycobacterium+tuberculosis%22">Mycobacterium tuberculosis</searchLink><br /><searchLink fieldCode="DE" term="%22Recombinant+proteins%22">Recombinant proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Crystallization%22">Crystallization</searchLink><br /><searchLink fieldCode="DE" term="%22Optical+diffraction%22">Optical diffraction</searchLink>
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  Data: Phosphoglucose isomerase is a ubiquitous enzyme that catalyzes the isomerization ofd-glucopyranose-6-phosphate tod-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 I212121, with unit-cell parameters a = 109.0, b = 119.8, c = 138.9 Å. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Acta Crystallographica: Section F (Wiley-Blackwell) is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1107/S1744309107013218
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      – Code: eng
        Text: English
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        Type: general
      – SubjectFull: Enzymes
        Type: general
      – SubjectFull: Mycobacterium tuberculosis
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      – SubjectFull: Recombinant proteins
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      – SubjectFull: Optical diffraction
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              Text: Apr2007
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