Source:http://linkedlifedata.com/resource/pubmed/id/15103152
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 5
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pubmed:dateCreated |
2004-4-22
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Flavoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Metronidazole,
http://linkedlifedata.com/resource/pubmed/chemical/Nitroglycerin,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Selenomethionine,
http://linkedlifedata.com/resource/pubmed/chemical/Trinitrotoluene,
http://linkedlifedata.com/resource/pubmed/chemical/XenA protein, Pseudomonas putida
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0907-4449
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
60
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
957-61
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pubmed:dateRevised |
2007-7-24
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pubmed:meshHeading |
pubmed-meshheading:15103152-Bacterial Proteins,
pubmed-meshheading:15103152-Catalytic Domain,
pubmed-meshheading:15103152-Crystallization,
pubmed-meshheading:15103152-Crystallography, X-Ray,
pubmed-meshheading:15103152-Flavoproteins,
pubmed-meshheading:15103152-Ligands,
pubmed-meshheading:15103152-Metronidazole,
pubmed-meshheading:15103152-Nitroglycerin,
pubmed-meshheading:15103152-Oxidoreductases,
pubmed-meshheading:15103152-Protein Conformation,
pubmed-meshheading:15103152-Pseudomonas putida,
pubmed-meshheading:15103152-Reproducibility of Results,
pubmed-meshheading:15103152-Selenomethionine,
pubmed-meshheading:15103152-Trinitrotoluene
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pubmed:year |
2004
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pubmed:articleTitle |
Crystallization and preliminary analysis of xenobiotic reductase A and ligand complexes from Pseudomonas putida II-B.
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pubmed:affiliation |
School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332-0400, USA. allen.orville@chemistry.gatech.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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