Source:http://linkedlifedata.com/resource/pubmed/id/16301799
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 12
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pubmed:dateCreated |
2005-11-22
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pubmed:abstractText |
A new crystal form of wild-type ribonucleotide reductase R2 from Escherichia coli was obtained. Crystals grow in space group P6(1)22 with one R2 monomer in the asymmetric unit. A twofold crystallographic symmetry axis generates the physiological dimeric form of R2. Co-crystallization with CoCl(2) or MnCl(2) results in full occupancy of the dinuclear metal site. The structure of the Mn(II)-loaded form was determined to 2.6 Angstroms resolution by molecular replacement. The crystallization conditions, backbone conformation, crystal-packing interactions and metal centers are compared with those of previously determined crystal forms.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0907-4449
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
61
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1649-54
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16301799-Binding Sites,
pubmed-meshheading:16301799-Crystallization,
pubmed-meshheading:16301799-Crystallography, X-Ray,
pubmed-meshheading:16301799-Escherichia coli,
pubmed-meshheading:16301799-Models, Molecular,
pubmed-meshheading:16301799-Protein Conformation,
pubmed-meshheading:16301799-Ribonucleotide Reductases
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pubmed:year |
2005
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pubmed:articleTitle |
Structure of Escherichia coli ribonucleotide reductase R2 in space group P6122.
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pubmed:affiliation |
Department of Biochemistry, Northwestern University, Evanston, IL 60208, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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