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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
|
pubmed:dateCreated |
1989-5-2
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pubmed:abstractText |
The gene coding for 3-isopropylmalate dehydrogenase of Thermus thermophilus was cloned and expressed in Escherichia coli. The extracted enzyme was crystallized in a suitable size for X-ray crystallographic studies. The crystals have a space group of P3(1)21 or P3(2)21 with a = b = 78.6 A and c = 157.4 A.
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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 |
Nov
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pubmed:issn |
0021-924X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
104
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
679-80
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pubmed:dateRevised |
2007-12-19
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pubmed:meshHeading |
pubmed-meshheading:3069841-3-Isopropylmalate Dehydrogenase,
pubmed-meshheading:3069841-Alcohol Oxidoreductases,
pubmed-meshheading:3069841-Crystallization,
pubmed-meshheading:3069841-Escherichia coli,
pubmed-meshheading:3069841-Recombinant Proteins,
pubmed-meshheading:3069841-Thermus,
pubmed-meshheading:3069841-X-Ray Diffraction
|
pubmed:year |
1988
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pubmed:articleTitle |
Crystallization and preliminary X-ray data for 3-isopropylmalate dehydrogenase of Thermus thermophilus.
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pubmed:affiliation |
Institute of Protein Research, Osaka University.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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