pubmed-article:20445270 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20445270 | lifeskim:mentions | umls-concept:C2313605 | lld:lifeskim |
pubmed-article:20445270 | lifeskim:mentions | umls-concept:C0009015 | lld:lifeskim |
pubmed-article:20445270 | lifeskim:mentions | umls-concept:C0043309 | lld:lifeskim |
pubmed-article:20445270 | lifeskim:mentions | umls-concept:C0010423 | lld:lifeskim |
pubmed-article:20445270 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:20445270 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
pubmed-article:20445270 | lifeskim:mentions | umls-concept:C0971052 | lld:lifeskim |
pubmed-article:20445270 | pubmed:issue | Pt 5 | lld:pubmed |
pubmed-article:20445270 | pubmed:dateCreated | 2010-5-6 | lld:pubmed |
pubmed-article:20445270 | pubmed:abstractText | Superoxide reductases (SORs) are metalloproteins which constitute the most recently identified oxygen-detoxification system in anaerobic and microaerobic bacteria and archaea. SORs are involved in scavenging superoxide radicals from the cell by catalyzing the reduction of superoxide ({\rm O}_{2};{\bullet -}) to hydrogen peroxide and are characterized by a catalytic nonhaem iron centre coordinated by four histidine ligands and one cysteine ligand. Ignicoccus hospitalis, a hyperthermophilic crenarchaeon, is known to have a neelaredoxin-type SOR that keeps toxic oxygen species levels under control. Blue crystals of recombinant I. hospitalis oxidized neelaredoxin (14.1 kDa, 124 residues) were obtained. These crystals diffracted to 2.4 A resolution in-house at room temperature and belonged to the hexagonal space group P6(2)22 or P6(4)22, with unit-cell parameters a = b = 108, c = 64 A. Cell-content analysis indicated the presence of one monomer in the asymmetric unit. | lld:pubmed |
pubmed-article:20445270 | pubmed:language | eng | lld:pubmed |
pubmed-article:20445270 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20445270 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:20445270 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20445270 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20445270 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20445270 | pubmed:month | May | lld:pubmed |
pubmed-article:20445270 | pubmed:issn | 1744-3091 | lld:pubmed |
pubmed-article:20445270 | pubmed:author | pubmed-author:TeixeiraMigue... | lld:pubmed |
pubmed-article:20445270 | pubmed:author | pubmed-author:HuberHaraldH | lld:pubmed |
pubmed-article:20445270 | pubmed:author | pubmed-author:MatiasPedro... | lld:pubmed |
pubmed-article:20445270 | pubmed:author | pubmed-author:RomãoCélia... | lld:pubmed |
pubmed-article:20445270 | pubmed:author | pubmed-author:SaraivaLígia... | lld:pubmed |
pubmed-article:20445270 | pubmed:author | pubmed-author:BandeirasTiag... | lld:pubmed |
pubmed-article:20445270 | pubmed:author | pubmed-author:PintoAna FAF | lld:pubmed |
pubmed-article:20445270 | pubmed:author | pubmed-author:PinhoFilipa... | lld:pubmed |
pubmed-article:20445270 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20445270 | pubmed:day | 1 | lld:pubmed |
pubmed-article:20445270 | pubmed:volume | 66 | lld:pubmed |
pubmed-article:20445270 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20445270 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20445270 | pubmed:pagination | 605-7 | lld:pubmed |
pubmed-article:20445270 | pubmed:meshHeading | pubmed-meshheading:20445270... | lld:pubmed |
pubmed-article:20445270 | pubmed:meshHeading | pubmed-meshheading:20445270... | lld:pubmed |
pubmed-article:20445270 | pubmed:meshHeading | pubmed-meshheading:20445270... | lld:pubmed |
pubmed-article:20445270 | pubmed:meshHeading | pubmed-meshheading:20445270... | lld:pubmed |
pubmed-article:20445270 | pubmed:meshHeading | pubmed-meshheading:20445270... | lld:pubmed |
pubmed-article:20445270 | pubmed:meshHeading | pubmed-meshheading:20445270... | lld:pubmed |
pubmed-article:20445270 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:20445270 | pubmed:articleTitle | Cloning, purification, crystallization and X-ray crystallographic analysis of Ignicoccus hospitalis neelaredoxin. | lld:pubmed |
pubmed-article:20445270 | pubmed:affiliation | Instituto de Biologia Experimental e Tecnológica, Apartado 12, 2701-901 Oeiras, Portugal. | lld:pubmed |
pubmed-article:20445270 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:20445270 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20445270 | lld:entrezgene |