Unknown

Dataset Information

0

Overexpression, purification and crystallization of a thermostable DNA ligase from the archaeon Thermococcus sp. 1519.


ABSTRACT: 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.

SUBMITTER: Bezsudnova EY 

PROVIDER: S-EPMC2664762 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

Overexpression, purification and crystallization of a thermostable DNA ligase from the archaeon Thermococcus sp. 1519.

Bezsudnova E Y EY   Kovalchuk M V MV   Mardanov A V AV   Poliakov K M KM   Popov V O VO   Ravin N V NV   Skryabin K G KG   Smagin V A VA   Stekhanova T N TN   Tikhonova T V TV  

Acta crystallographica. Section F, Structural biology and crystallization communications 20090325 Pt 4


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 bel  ...[more]

Similar Datasets

| S-EPMC3274393 | biostudies-literature
| S-EPMC2882762 | biostudies-literature
| S-EPMC91287 | biostudies-literature
| S-EPMC1978129 | biostudies-literature
| S-EPMC8146568 | biostudies-literature
| S-EPMC93801 | biostudies-literature
| S-EPMC3509962 | biostudies-literature
| S-EPMC2593222 | biostudies-literature
| S-EPMC22340 | biostudies-literature
| S-EPMC1393192 | biostudies-literature