pubmed-article:15103152 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15103152 | lifeskim:mentions | umls-concept:C0085470 | lld:lifeskim |
pubmed-article:15103152 | lifeskim:mentions | umls-concept:C0030016 | lld:lifeskim |
pubmed-article:15103152 | lifeskim:mentions | umls-concept:C0043335 | lld:lifeskim |
pubmed-article:15103152 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
pubmed-article:15103152 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
pubmed-article:15103152 | lifeskim:mentions | umls-concept:C0010423 | lld:lifeskim |
pubmed-article:15103152 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:15103152 | lifeskim:mentions | umls-concept:C0439611 | lld:lifeskim |
pubmed-article:15103152 | pubmed:issue | Pt 5 | lld:pubmed |
pubmed-article:15103152 | pubmed:dateCreated | 2004-4-22 | lld:pubmed |
pubmed-article:15103152 | pubmed:abstractText | Diffraction-quality crystals have been obtained of the xenobiotic reductase A (XenA) from Pseudomonas II-B, which was originally cultured from the contaminated soil of a World War II era munitions-manufacturing plant. Several complete X-ray diffraction data sets have been collected and analyzed. The native XenA data set includes reflections between 35 and 1.65 A. Four-wavelength MAD data sets from selenomethionine-enriched XenA and from three different ligand complexes are also reported. The XenA crystals belong to space group P2(1)2(1)2, with unit-cell parameters a = 84, b = 158, c = 57 A. Experimental phasing from analysis of the MAD data from selenomethionine-enriched XenA reveals the presence of two molecules in the asymmetric unit. They are related by a non-crystallographic 2(1) screw axis nearly parallel to the c axis, but offset by a quarter unit-cell translation. Thus, the local symmetry produces approximate systematic absences along the (00l) principal axis and complicates the space-group determination. | lld:pubmed |
pubmed-article:15103152 | pubmed:language | eng | lld:pubmed |
pubmed-article:15103152 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15103152 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:15103152 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15103152 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15103152 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15103152 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15103152 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15103152 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15103152 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15103152 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15103152 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15103152 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15103152 | pubmed:month | May | lld:pubmed |
pubmed-article:15103152 | pubmed:issn | 0907-4449 | lld:pubmed |
pubmed-article:15103152 | pubmed:author | pubmed-author:FischerT FTF | lld:pubmed |
pubmed-article:15103152 | pubmed:author | pubmed-author:StudtsJoey... | lld:pubmed |
pubmed-article:15103152 | pubmed:author | pubmed-author:FoxBrian GBG | lld:pubmed |
pubmed-article:15103152 | pubmed:author | pubmed-author:BlehertDavid... | lld:pubmed |
pubmed-article:15103152 | pubmed:author | pubmed-author:ChamblissGlen... | lld:pubmed |
pubmed-article:15103152 | pubmed:author | pubmed-author:ManningLindaL | lld:pubmed |
pubmed-article:15103152 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15103152 | pubmed:volume | 60 | lld:pubmed |
pubmed-article:15103152 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15103152 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15103152 | pubmed:pagination | 957-61 | lld:pubmed |
pubmed-article:15103152 | pubmed:dateRevised | 2007-7-24 | lld:pubmed |
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pubmed-article:15103152 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:15103152 | pubmed:articleTitle | Crystallization and preliminary analysis of xenobiotic reductase A and ligand complexes from Pseudomonas putida II-B. | lld:pubmed |
pubmed-article:15103152 | pubmed:affiliation | School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332-0400, USA. allen.orville@chemistry.gatech.edu | lld:pubmed |
pubmed-article:15103152 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15103152 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:15103152 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:15103152 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |