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한국구조생물학회 Biodesign Biodesign 제7권 제1호
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    초록·키워드

    Sirtuins are NAD+-dependent deacetylase that are broadly conserved throughout bacteria, archaea, and eukaryotes. Themembers of sirtuins are important in regulating diverse biological pathways, including gene silencing, DNA repair, genomestability, longevity, metabolism, and cell physiology. Sirtuin from Bacillus amyloliquefaciens (BaSrtN) is a particularlyinteresting bacterial Sir2 homologue. In this study, to further understand the function and mechanisms of this protein,BaSrtN was successfully expressed and purified using Ni-NTA affinity, Q anion-exchange, and gel-filtration chromatography. Purified BaSrtN was crystallized and diffracted to the resolution of 1.45 Å. The preliminary crystallographic analysissuggested that BaSrtN crystal belongs to the trigonal space group P31 or P32, with unit-cell parameters of a = b = 90.115and c = 86.306 Å. Size-exclusion chromatography suggested that BaSrtN prefer to exit as monomers in solution.

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