DC Field | Value | Language |
---|---|---|
dc.contributor.author | Uyen, NT | - |
dc.contributor.author | Nishi, K | - |
dc.contributor.author | Park, SY | - |
dc.contributor.author | Choi, JW | - |
dc.contributor.author | Lee, HJ | - |
dc.contributor.author | Kim, JS | - |
dc.date.accessioned | 2022-01-10T06:40:19Z | - |
dc.date.available | 2022-01-10T06:40:19Z | - |
dc.date.created | 2021-07-05 | - |
dc.date.issued | 2008-10 | - |
dc.identifier.issn | 1744-3091 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/109132 | - |
dc.description.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%. | - |
dc.language | English | - |
dc.publisher | International Union of Crystallography | - |
dc.relation.isPartOf | Acta Crystallographica Section F: Structural Biology and Crystallization Communications | - |
dc.title | Crystallization and preliminary X-ray diffraction analysis of the HsdR subunit of a putative type I restriction enzyme from Vibrio vulnificus YJ016 | - |
dc.type | Article | - |
dc.identifier.doi | 10.1107/S1744309108027516 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | Acta Crystallographica Section F: Structural Biology and Crystallization Communications, v.64, no.10, pp.926 - 928 | - |
dc.identifier.wosid | 000260008100011 | - |
dc.citation.endPage | 928 | - |
dc.citation.number | 10 | - |
dc.citation.startPage | 926 | - |
dc.citation.title | Acta Crystallographica Section F: Structural Biology and Crystallization Communications | - |
dc.citation.volume | 64 | - |
dc.contributor.affiliatedAuthor | Park, SY | - |
dc.identifier.scopusid | 2-s2.0-53749084424 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.type.docType | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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