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| Title: | Purification, crystallization and preliminary structural analysis of nucleoside diphosphate kinase from Bacillus anthracis |
| Authors: | Misra, Gauri
Aggarwal, Anita
Mittal, Sonia
Singh, Yogendra
Ravishankar, Ramachandran |
| Issue Date: | 2007 |
| Citation: | Acta Crystallographica Section F(2007), F63, 1084-1086 |
| Series/Report no.: | CDRI communication No. 7390 |
| Abstract: | Bacillus anthracis nucleoside diphosphate kinase (BaNdk) is an enzyme whose
primary function is to maintain deoxynucleotide triphosphate (dNTP) pools by
converting deoxynucleotide diphosphates to triphosphates using ATP as the
major phosphate donor. Although the structures of Ndks from a variety of
organisms have been elucidated, the enzyme from sporulating bacteria has not
been structurally characterized to date. Crystals of the B. anthracis enzyme were
grown using the vapour-diffusion method from a hanging drop consisting of 2 ml
10 mg ml1 protein in 50 mM Tris–HCl pH 8.0, 50 mM NaCl, 5 mM EDTA
equilibrated against 500 ml reservoir solution consisting of 2.25 M ammonium
formate and 0.1 M HEPES buffer pH 7.25. Diffraction data extending to 2.0 A ˚
were collected at room temperature from a single crystal with unit-cell
parameters a = b = 107.53, c = 52.3 A ˚ . The crystals are hexagonal in shape and
belong to space group P6322. The crystals contain a monomer in the asymmetric
unit, which corresponds to a Matthews coefficient (VM) of 2.1 A ˚ 3 Da1 and a
solvent content of about 36.9%. |
| URI: | http://hdl.handle.net/123456789/131 |
| Appears in Collections: | Molecular & Structural Biology
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| rravi-actacrystallo-F63-1084-2007.pdf | | 348Kb | Adobe PDF | View/Open |
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