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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1976-3-18
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pubmed:abstractText |
16-S ribosomal RNA and a complex of ribosomal protein S4 and 16-S rRNA were studied in solution by small-angle X-ray scattering. Concentration series of the 16-S rRNA and the S4 - 16-S-rRNA complex were measured in 37.5 mM Tris-HCl buffer pH 7.4 at 5 degrees C. The following data were determined. The radii of gyration for the 16-S rRNA and S4 - 16-S-rRNA complex were R = 17.6 +/- 0.6 nm, respectively. The two respective values of the radii of gyration of the cross-section were Rq,1 = 8.42 +/- 0.1 nm and 8.33 +/- 0.3 nm, and Rq,2 = 0.988 +/- 0.03 nm and 0.996 +/- 0.03 nm. The largest diameters of the 16-S RNA and S4 - 16-S-RNA complex were L = 61.8 +/- 1 nm and 60.0 +/- 1 nm, respectively. Volumes of V = 1570 +/- 60 nm3 were found for both particles. In the Tris buffer used, no significant differences were found between the scattering curves of 16-S rRNA and the complex is a flat elliptical cylinder with the following dimensions: large axis 61.7 nm, small axis 35.4 nm and height 2 nm. The theoretical scattering curve fits the experimental one as long as the shape of the measured curve is due only to the overall shape of the particle. A model equivalent over the whole measured angular range is one built up from a large number of spheres that simulate the known substructure of the RNA. The outer dimensions of this model correspond to those of the flat elliptical cylinder.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
59
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
63-71
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:1107026-Bacterial Proteins,
pubmed-meshheading:1107026-Binding Sites,
pubmed-meshheading:1107026-Deoxyribonucleoproteins,
pubmed-meshheading:1107026-Escherichia coli,
pubmed-meshheading:1107026-Macromolecular Substances,
pubmed-meshheading:1107026-Models, Molecular,
pubmed-meshheading:1107026-Nucleoproteins,
pubmed-meshheading:1107026-Protein Binding,
pubmed-meshheading:1107026-Protein Conformation,
pubmed-meshheading:1107026-RNA, Ribosomal,
pubmed-meshheading:1107026-Ribosomal Proteins,
pubmed-meshheading:1107026-X-Ray Diffraction
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pubmed:year |
1975
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pubmed:articleTitle |
Small-angle x-ray studies on the structure of 16-S ribosomal RNA and of a complex of ribosomal protein S4 and 16-S ribosomal RNA from Escherichia coli.
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pubmed:publicationType |
Journal Article
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