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DNA ligases catalyze the sealing of 5 0 -phosphate and 3 0 -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 vapourdiffusion method employing 35%(v/v) Tacsimate pH 7.0 as a precipitant and diffracted X-rays to 3.09 Å resolution. They belonged to space group P4 1 2 1 2, with unit-cell parameters a = b = 79.7, c = 182.6 Å .

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