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| Title: | Overexpression, purification, crystallization and preliminary X-ray analysis of Rv2780 from Mycobacterium tuberculosis H37Rv |
| Authors: | Tripathi, Sarvind Mani
Ravishankar, Ramachandran |
| Issue Date: | 2008 |
| Citation: | Acta Cryst. (2008). F64, 367–370 |
| Series/Report no.: | CDRI Communication No 7472 |
| Abstract: | Rv2780, an alanine dehydrogenase from Mycobacterium tuberculosis
(MtAlaDH), catalyzes the NAD-dependent interconversion of alanine and
pyruvate. Alanine dehydrogenase is released into the culture medium in
substantial amounts by virulent strains of mycobacteria and is not found in the
vaccine strain of tuberculosis. Crystals of recombinant MtAlaDH were grown
from 2 M ammonium sulfate solution at 12 mg ml1 protein concentration in
two crystal forms which occur in the presence and absence of NAD/pyruvate,
respectively. Diffraction data extending to 2.6 A ˚ were collected at room
temperature from both apo and ternary complex crystals. Crystals of the
apoenzyme have unit-cell parameters a = 173.89, b = 127.07, c = 135.95 A ˚ . They
are rod-like in shape and belong to space group C2. They contain a hexamer in
the asymmetric unit. Crystals of the ternary complex belong to space group
P43212 and have unit-cell parameters a = b = 88.99, c = 373.85 A ˚ . There are three
subunits in the asymmetric unit of the holoenzyme crystals. |
| URI: | http://hdl.handle.net/123456789/132 |
| Appears in Collections: | Molecular & Structural Biology
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| rravi-actacrystallo-F64-367-2008.pdf | | 342Kb | Adobe PDF | View/Open |
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