Source:http://linkedlifedata.com/resource/pubmed/id/15299591
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
Pt 6
|
| pubmed:dateCreated |
2004-8-9
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| pubmed:abstractText |
DNA gyrase B (GyrB) from B. stearothermophilus has been crystallized in the presence of the non-hydrolyzable ATP analogue, 5'-adenylyl-beta-gamma-imidodiphosphate (ADPNP), by the dialysis method. A complete native data set to 3.7 A has been collected from crystals which belonged to the cubic space group I23 with unit-cell dimension a = 250.6 A. Self-rotation function analysis indicates the position of a molecular twofold axis. Low-resolution data sets of a thimerosal and a selenomethionine derivative have also been analysed. The heavy-atom positions are consistent with one dimer in the asymmetric unit.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:status |
PubMed-not-MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0907-4449
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
|
| pubmed:volume |
52
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1216-8
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| pubmed:dateRevised |
2007-7-24
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| pubmed:year |
1996
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| pubmed:articleTitle |
Crystallization and preliminary crystallographic analysis of the DNA gyrase B protein from B. stearothermophilus.
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| pubmed:affiliation |
Laboratory of Molecular Biophysics, University of Oxford, England.
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| pubmed:publicationType |
Journal Article
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