Journal Article PHPPUBDB-20240

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

 ;  ;  ;  ;  ;  ;  ;  ;  ;  ; DESY

2009
Blackwell Oxford [u.a.]

Acta crystallographica / F 65, 368-371 () [10.1107/S1744309109007799]
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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.

Keyword(s): Crystallization (MeSH) ; Crystallography, X-Ray (MeSH) ; DNA Ligases: chemistry (MeSH) ; DNA Ligases: isolation & purification (MeSH) ; Electrophoresis, Polyacrylamide Gel (MeSH) ; Enzyme Stability (MeSH) ; Recombinant Proteins: chemistry (MeSH) ; Recombinant Proteins: isolation & purification (MeSH) ; Temperature (MeSH) ; Thermococcus: enzymology (MeSH) ; Recombinant Proteins ; DNA Ligases

Classification:

Contributing Institute(s):
  1. European Molecular Biology Laboratory (EMBL)
Research Program(s):
  1. DORIS Beamline K1.1 (POF1-550) (POF1-550)
Experiment(s):
  1. DORIS Beamline K1.1 (DORIS III)

Appears in the scientific report 2009
Database coverage:
Medline ; JCR ; No Author Disambiguation ; Thomson Reuters Master Journal List ; Web of Science Core Collection
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 Record created 2012-09-19, last modified 2025-07-31


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