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rdf:type |
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lifeskim:mentions |
umls-concept:C0010423,
umls-concept:C0017262,
umls-concept:C0031727,
umls-concept:C0042567,
umls-concept:C0051612,
umls-concept:C0085471,
umls-concept:C0185117,
umls-concept:C0205314,
umls-concept:C0439611,
umls-concept:C0679622,
umls-concept:C1334043,
umls-concept:C1540311,
umls-concept:C2603343,
umls-concept:C2911684
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pubmed:issue |
Pt 12
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pubmed:dateCreated |
2006-12-4
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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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-10393305,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-10508770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-12005432,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-12049647,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-12459178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-12594532,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-12633501,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-12754705,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-13525417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-13563449,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-15062076,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-15325649,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-16122935,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-16321554,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-16376937,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-170089,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-3534538,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-5700707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-6885773,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-8373783,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-9572954,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142901-9806879
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1744-3091
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
62
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1218-22
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
2006
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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.
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pubmed:affiliation |
Children's National Medical Center, The George Washington University, 111 Michigan Avenue, Washington, DC 20010, USA. dshi@cnmcresearch.org
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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