Source:http://linkedlifedata.com/resource/pubmed/id/15299914
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 4
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pubmed:dateCreated |
2004-8-9
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pubmed:abstractText |
Electron-transferring flavoprotein from the rumen bacterium Megasphaera elsdenii is a heterodimer (M(r) = 75 kDa) containing FAD as cofactor and functioning solely to mediate electron transfer between the prosthetic groups of other proteins. The enzyme was crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 4000 as precipitant. The crystals obtained belong to the space group P2(1)2(1)2(1) with unit-cell dimensions of a = 58.75, b = 61.77 and c = 122.27 A. Interestingly the crystals exhibit a low solvent content. Crystals diffracted to beyond 2.5 A using synchrotron radiation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:status |
PubMed-not-MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0907-4449
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
53
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
461-3
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pubmed:dateRevised |
2007-7-24
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pubmed:year |
1997
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pubmed:articleTitle |
Crystallization and preliminary X-ray crystallographic analysis of the electron-transferring flavoprotein from Megasphaera elsdenii.
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pubmed:affiliation |
Department of Chemistry, University College, Galway, Ireland.
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pubmed:publicationType |
Journal Article
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