pubmed-article:17142901 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17142901 | lifeskim:mentions | umls-concept:C0085471 | lld:lifeskim |
pubmed-article:17142901 | lifeskim:mentions | umls-concept:C0042567 | lld:lifeskim |
pubmed-article:17142901 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
pubmed-article:17142901 | lifeskim:mentions | umls-concept:C0051612 | lld:lifeskim |
pubmed-article:17142901 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:17142901 | lifeskim:mentions | umls-concept:C1540311 | lld:lifeskim |
pubmed-article:17142901 | lifeskim:mentions | umls-concept:C0010423 | lld:lifeskim |
pubmed-article:17142901 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
pubmed-article:17142901 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:17142901 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:17142901 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
pubmed-article:17142901 | lifeskim:mentions | umls-concept:C0439611 | lld:lifeskim |
pubmed-article:17142901 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
pubmed-article:17142901 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
pubmed-article:17142901 | pubmed:issue | Pt 12 | lld:pubmed |
pubmed-article:17142901 | pubmed:dateCreated | 2006-12-4 | lld:pubmed |
pubmed-article:17142901 | pubmed:abstractText | A novel N-acetylglutamate synthase/kinase bifunctional enzyme of arginine biosynthesis that was homologous to vertebrate N-acetylglutamate synthases was identified in Xanthomonas campestris. The protein was overexpressed, purified and crystallized. The crystals belong to the hexagonal space group P6(2)22, with unit-cell parameters a = b = 134.60, c = 192.11 A, and diffract to about 3.0 A resolution. Selenomethionine-substituted recombinant protein was produced and selenomethionine substitution was verified by mass spectroscopy. Multiple anomalous dispersion (MAD) data were collected at three wavelengths at SER-CAT, Advanced Photon Source, Argonne National Laboratory. Structure determination is under way using the MAD phasing method. | lld:pubmed |
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pubmed-article:17142901 | pubmed:language | eng | lld:pubmed |
pubmed-article:17142901 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17142901 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:17142901 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17142901 | pubmed:month | Dec | lld:pubmed |
pubmed-article:17142901 | pubmed:issn | 1744-3091 | lld:pubmed |
pubmed-article:17142901 | pubmed:author | pubmed-author:TuchmanMendel... | lld:pubmed |
pubmed-article:17142901 | pubmed:author | pubmed-author:MorizonoHirok... | lld:pubmed |
pubmed-article:17142901 | pubmed:author | pubmed-author:HathoutYetrib... | lld:pubmed |
pubmed-article:17142901 | pubmed:author | pubmed-author:CaldovicLjubi... | lld:pubmed |
pubmed-article:17142901 | pubmed:author | pubmed-author:YuXiaolinX | lld:pubmed |
pubmed-article:17142901 | pubmed:author | pubmed-author:ShiDashuangD | lld:pubmed |
pubmed-article:17142901 | pubmed:author | pubmed-author:AllewellNorma... | lld:pubmed |
pubmed-article:17142901 | pubmed:author | pubmed-author:QuQiuhaoQ | lld:pubmed |
pubmed-article:17142901 | pubmed:author | pubmed-author:JinZhongminZ | lld:pubmed |
pubmed-article:17142901 | pubmed:author | pubmed-author:RothLaurenL | lld:pubmed |
pubmed-article:17142901 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:17142901 | pubmed:day | 1 | lld:pubmed |
pubmed-article:17142901 | pubmed:volume | 62 | lld:pubmed |
pubmed-article:17142901 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17142901 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17142901 | pubmed:pagination | 1218-22 | lld:pubmed |
pubmed-article:17142901 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:17142901 | pubmed:meshHeading | pubmed-meshheading:17142901... | lld:pubmed |
pubmed-article:17142901 | pubmed:meshHeading | pubmed-meshheading:17142901... | lld:pubmed |
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pubmed-article:17142901 | pubmed:meshHeading | pubmed-meshheading:17142901... | lld:pubmed |
pubmed-article:17142901 | pubmed:meshHeading | pubmed-meshheading:17142901... | lld:pubmed |
pubmed-article:17142901 | pubmed:meshHeading | pubmed-meshheading:17142901... | lld:pubmed |
pubmed-article:17142901 | pubmed:meshHeading | pubmed-meshheading:17142901... | lld:pubmed |
pubmed-article:17142901 | pubmed:year | 2006 | lld:pubmed |
pubmed-article:17142901 | pubmed:articleTitle | Expression, crystallization and preliminary crystallographic studies of a novel bifunctional N-acetylglutamate synthase/kinase from Xanthomonas campestris homologous to vertebrate N-acetylglutamate synthase. | lld:pubmed |
pubmed-article:17142901 | pubmed:affiliation | Children's National Medical Center, The George Washington University, 111 Michigan Avenue, Washington, DC 20010, USA. dshi@cnmcresearch.org | lld:pubmed |
pubmed-article:17142901 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17142901 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:17142901 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17142901 | lld:entrezgene |
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