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. |
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| 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] |
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| Database: | Engineering Source |
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