Sirtuins are NAD + -dependent deacetylase that are broadly conserved throughout bacteria, archaea, and eukaryotes. The members of sirtuins are important in regulating diverse biological pathways, including gene silencing, DNA repair, genome stability, longevity, metabolism, and cell physiology. Sirtuin from Bacillus amyloliquefaciens (BaSrtN) is a particularly interesting 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 analysis suggested that BaSrtN crystal belongs to the trigonal space group P3 1 or P3 2 , with unit-cell parameters of a = b = 90.115 and c = 86.306 Å. Size-exclusion chromatography suggested that BaSrtN prefer to exit as monomers in solution.
INTRODUCTION
RESULTS AND DISCUSSION
METHODS