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Literature summary for 3.1.21.3 extracted from

  • Uyen, N.T.; Nishi, K.; Park, S.Y.; Choi, J.W.; Lee, H.J.; Kim, J.S.
    Crystallization and preliminary X-ray diffraction analysis of the HsdR subunit of a putative type I restriction enzyme from Vibrio vulnificus YJ016 (2008), Acta Crystallogr. Sect. F, 64, 926-928.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
HsdR subunit cloned into pProExHTc and expressed in Escherichia coli B834(DE3) Vibrio vulnificus YJ016

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop and sitting-drop vapour-diffusion method, HsdR subunit 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, to 2.60 A resolution. 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 molecule in the asymmetric unit, the Matthews coefficient is 2.14 A3 Da-1 and the solvent content is 42% Vibrio vulnificus YJ016

Organism

Organism UniProt Comment Textmining
Vibrio vulnificus YJ016
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-
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Purification (Commentary)

Purification (Comment) Organism
HsdR fusion protein purified by gel filtration. HsdR with five additional amino acids (YFQGA) at the N-terminus purified on anion-exchange column and by gel filtration, purified protein is more than 95% pure Vibrio vulnificus YJ016

Synonyms

Synonyms Comment Organism
type I restriction enzyme
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Vibrio vulnificus YJ016