Overexpression, purification and crystallization of a thermostable DNA ligase from the archaeon Thermococcus sp. 1519.
- Bezsudnova, E. Y.
- Kovalchuk, M. V.
- Mardanov, A. V.
- Poliakov, K. M.
- Popov, V. O.
- Ravin, N. V.
- Skryabin, K. G.
- Smagin, V. A.
- Stekhanova, T. N.
- Tikhonova, T. V.
DOIAbstract
DNA ligases catalyze the sealing of 5'-phosphate and 3'-hydroxyl termini at single-strand breaks in double-stranded DNA and their function is essential to maintain the integrity of the genome in DNA metabolism. An ATP-dependent DNA ligase from the archaeon Thermococcus sp. 1519 was overexpressed, purified and crystallized. Crystals were obtained using the hanging-drop vapour-diffusion method employing 35%(v/v) Tacsimate pH 7.0 as a precipitant and diffracted X-rays to 3.09 A resolution. They belonged to space group P4(1)2(1)2, with unit-cell parameters a = b = 79.7, c = 182.6 A
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