Source:http://linkedlifedata.com/resource/pubmed/id/11264599
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 4
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pubmed:dateCreated |
2001-3-26
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pubmed:abstractText |
Thermostable alkaline phosphatase from Thermus sp. 3041 has been expressed in Escherichia coli, purified and crystallized. The crystals belong to space group P2(1)22(1), with unit-cell parameters a = 57.7, b = 69.9, c = 111.5 A. Diffraction data were collected to 2.54 A with a completeness of 91.1% (87.8% for the last shell), an R(merge) value of 0.105 (0.312) and an I/sigma(I) value of 9.5 (3.6).
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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 |
Apr
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pubmed:issn |
0907-4449
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
57
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
614-5
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pubmed:dateRevised |
2007-7-24
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pubmed:meshHeading |
pubmed-meshheading:11264599-Alkaline Phosphatase,
pubmed-meshheading:11264599-Crystallization,
pubmed-meshheading:11264599-Enzyme Stability,
pubmed-meshheading:11264599-Recombinant Proteins,
pubmed-meshheading:11264599-Structure-Activity Relationship,
pubmed-meshheading:11264599-Temperature,
pubmed-meshheading:11264599-Thermus,
pubmed-meshheading:11264599-X-Ray Diffraction
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pubmed:year |
2001
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pubmed:articleTitle |
Purification, crystallization and preliminary X-ray studies of thermostable alkaline phosphatase from Thermus sp. 3041.
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pubmed:affiliation |
Institute of Genetics, School of Life Science, Fudan University, Shanghai, People's Republic of China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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