Source:http://linkedlifedata.com/resource/pubmed/id/10089375
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 2
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pubmed:dateCreated |
1999-4-15
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pubmed:abstractText |
The flavoenzyme L-aspartate oxidase from Escherichia coli was crystallized using the hanging-drop vapour-diffusion technique with PEG 4000 as precipitant. The crystals belong to space group P3121 (or P3221) with unit-cell parameters a = b = 84.9, c = 159.9 A. A solvent content of 42% corresponds to a monomer (60 kDa) in the asymmetric unit. A complete 2.8 A resolution data set was collected using a rotating-anode X-ray generator.
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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 |
Feb
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pubmed:issn |
0907-4449
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
55
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
549-51
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pubmed:dateRevised |
2007-7-24
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pubmed:meshHeading | |
pubmed:year |
1999
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pubmed:articleTitle |
Crystallization of L-aspartate oxidase, the first enzyme in the bacterial de novo biosynthesis of NAD.
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pubmed:affiliation |
Dipartimento di Genetica e Microbiologia, Università di Pavia, Via Abbiategrasso 207, 27100 Pavia, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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