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  The Molecular Architecture of the Extracellular Hemoglobin of Ophelia bicornis: Analysis of Individual Molecules

Cejka, Z., Kleinz, J., Santini, C., Hegerl, R., & Ghiretti Magaldi, A. (1992). The Molecular Architecture of the Extracellular Hemoglobin of Ophelia bicornis: Analysis of Individual Molecules. J. Struct. Biol., 109(1), 52-60.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-7419-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-741A-3
Genre: Journal Article

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Cejka, Z., Author
Kleinz, J., Author
Santini, C., Author
Hegerl, R.1, Author              
Ghiretti Magaldi, A., Author
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1External Organizations, ou_persistent22              

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 Abstract: The dimensions and shape of extracellular hemoglobin molecules of the marine worm, Ophelia bicornis, were determined by electron microscopy using negative staining and embedding in aurothioglucose. The typical averaged double-layered hexagon has a diameter of 26.5 nm and a height of 18 nm. The three-dimensional reconstruction of the negatively stained samples, using random conical tilting, showed about 60% of the original height of the molecule due to flattening and incomplete embedding in stain. In contrast to this, the specimen embedded in aurothioglucose showed no flattening. The three-dimensional reconstructions agree with the structure found in a previous study on 2-D crystalline arrays. In particular, the main subunit shows more than three mass centers.

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 Dates: 1992
 Publication Status: Published in print
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 Identifiers: eDoc: 318444
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Title: J. Struct. Biol.
Source Genre: Journal
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Pages: - Volume / Issue: 109 (1) Sequence Number: - Start / End Page: 52 - 60 Identifier: -