Crystallization and preliminary X-ray diffraction analysis of the HsdR subunit of a putative type I restriction enzyme from Vibrio vulnificus YJ016
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- Title
- Crystallization and preliminary X-ray diffraction analysis of the HsdR subunit of a putative type I restriction enzyme from Vibrio vulnificus YJ016
- Authors
- Uyen, NT; Nishi, K; Park, SY; Choi, JW; Lee, HJ; Kim, JS
- Date Issued
- 2008-10
- Publisher
- International Union of Crystallography
- Abstract
- Type I restriction enzymes are multimeric proteins that consist of three subunits. The HsdS and HsdM subunits form a complex protein that shows methyltransferase activity, while the HsdR subunit functions as an endonuclease as well as as a translocase. Of these three subunits, no structural information on the HsdR subunit is yet available. The putative HsdR gene from Vibrio vulnificus YJ016 (HsdR_Vv) was cloned and expressed and the expressed protein HsdR_Vv was purified. HsdR_Vv was crystallized from 8%(w/v) polyethylene glycol 3350, 0.15 M ammonium chloride, 0.1 M HEPES pH 7.5 and 2 mM beta-mercaptoethanol. Diffraction data were collected to 2.60 angstrom resolution using synchrotron radiation. The crystal belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 71.01, b = 89.04, c = 113.66 angstrom. With one HsdR_Vv molecule in the asymmetric unit, the Matthews coefficient was 2.14 angstrom(3) Da(-1) and the solvent content was 42%.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/109132
- DOI
- 10.1107/S1744309108027516
- ISSN
- 1744-3091
- Article Type
- Article
- Citation
- Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 64, no. 10, page. 926 - 928, 2008-10
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