ArticleActa crystallographica. Section F, Structural biology and crystallization communications2008
Crystallization and preliminary X-ray diffraction analysis of the HsdR subunit of a putative type I restriction enzyme from Vibrio vulnificus YJ016.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed.
- Type I restriction enzymes and their relatives.Nucleic acids research · 2014Review
- The fragment structure of a putative HsdR subunit of a type I restriction enzyme from Vibrio vulnificus YJ016: implications for DNA restriction and translocation activity.Nucleic acids research · 2009Article
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6 authors.
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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 A 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 A. With one HsdR_Vv molecule in the asymmetric unit, the Matthews coefficient was 2.14 A(3) Da(-1) and the solvent content was 42%.
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