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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1985-2-14
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pubmed:abstractText |
The crystal structure of a small calcium-binding protein, the parvalbumin IIIf from Opsanus tau in which Tb was substituted for Ca, has been analysed by multiwavelength anomalous diffraction. Data at a resolution of 2.3 A were collected at three wavelengths near the L3 absorption edge of Tb (1.645-1.650 A), using the synchrotron radiation emitted by a storage ring and a multiwire proportional counter. The phases of the reflections were determined from this single derivative, without native data. Prior to any refinement, the resulting electron density map shows a good agreement with the model of the homologous carp parvalbumin in regions of identical amino-acid sequence.
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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 |
Jan
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
179
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
133-7
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:3965297-Animals,
pubmed-meshheading:3965297-Carps,
pubmed-meshheading:3965297-Fishes,
pubmed-meshheading:3965297-Models, Molecular,
pubmed-meshheading:3965297-Muscle Proteins,
pubmed-meshheading:3965297-Parvalbumins,
pubmed-meshheading:3965297-Protein Conformation,
pubmed-meshheading:3965297-Species Specificity,
pubmed-meshheading:3965297-X-Ray Diffraction
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pubmed:year |
1985
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pubmed:articleTitle |
Crystal structure study of Opsanus tau parvalbumin by multiwavelength anomalous diffraction.
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pubmed:publicationType |
Journal Article
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