pISSN 2288-6982
eISSN 2288-7105




BioDesign 2019; 7(1): 19-23

Published online March 30, 2019

© Korean Society for Structural Biology

Bacillus amyloliquefaciens NAD+-dependent protein deacetylase: purification, crystallization and X-ray crystallographic analysis

Fei Shang1,2, Jinli Chen1,2, Lulu Wang1,2,3, Yuanyuan Chen1,2, Jing Lan1,2, Wei Liu1,2, Liming Jin1,2, Nam-Chul Ha4, Chunshan Quan1,2,* and Yongbin Xu1,2,*

1Department of Bioengineering, College of Life Science, Dalian Minzu University, Dalian 116600, Liaoning, China, 2Key Laboratory of Biotechnology and Bioresources Utilization (Dalian Minzu University), Ministry of Education, China, 3School of Life Science and Biotechnology, Dalian University of Technology, No 2 Linggong Road, Dalian 116024, Liaoning, China, 4Department of Agricultural Biotechnology, College of Agriculture and Life Sciences, Seoul National University, Gwanak-gu, Seoul 08826, Republic of Korea *Correspondence:,


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 P31 or P32, 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.