Two-dimensional crystals of streptavidin on biotinylated lipid layers and their interactions with biotinylated macromolecules
Streptavidin forms two-dimensional crystals when specifically bound to layers of biotinylated lipids at the air/water interface. The three-dimensional structure of streptavidin determined from the crystals by electron crystallography corresponds well with the structure determined by x-ray crystallog...
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| Veröffentlicht in: | Biophysical journal 1991-02, Vol.59 (2), p.387-396 |
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| container_title | Biophysical journal |
| container_volume | 59 |
| creator | Darst, S.A. Ahlers, M. Meller, P.H. Kubalek, E.W. Blankenburg, R. Ribi, H.O. Ringsdorf, H. Kornberg, R.D. |
| description | Streptavidin forms two-dimensional crystals when specifically bound to layers of biotinylated lipids at the air/water interface. The three-dimensional structure of streptavidin determined from the crystals by electron crystallography corresponds well with the structure determined by x-ray crystallography. Comparison of the electron and x-ray crystallographic structures reveals the occurrence of free biotin-binding sites on the surface of the two-dimensional crystals facing the aqueous solution. The free biotin-binding sites could be specifically labeled with biotinylated ferritin. The streptavidin/biotinylated lipid system may provide a general approach for the formation of two-dimensional crystals of biotinylated macromolecules. |
| doi_str_mv | 10.1016/S0006-3495(91)82232-9 |
| format | Article |
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The three-dimensional structure of streptavidin determined from the crystals by electron crystallography corresponds well with the structure determined by x-ray crystallography. Comparison of the electron and x-ray crystallographic structures reveals the occurrence of free biotin-binding sites on the surface of the two-dimensional crystals facing the aqueous solution. The free biotin-binding sites could be specifically labeled with biotinylated ferritin. 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The three-dimensional structure of streptavidin determined from the crystals by electron crystallography corresponds well with the structure determined by x-ray crystallography. Comparison of the electron and x-ray crystallographic structures reveals the occurrence of free biotin-binding sites on the surface of the two-dimensional crystals facing the aqueous solution. The free biotin-binding sites could be specifically labeled with biotinylated ferritin. The streptavidin/biotinylated lipid system may provide a general approach for the formation of two-dimensional crystals of biotinylated macromolecules.</description><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacterial Proteins - ultrastructure</subject><subject>Binding Sites</subject><subject>Biotin - metabolism</subject><subject>Fluorescein-5-isothiocyanate</subject><subject>Fluoresceins</subject><subject>Fluorescent Dyes</subject><subject>Liposomes</subject><subject>Microscopy, Electron</subject><subject>Models, Structural</subject><subject>Molecular Conformation</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Streptavidin</subject><subject>Thiocyanates</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUctuEzEUtRCohMInVPIKwWLAj3jG3oCqCtpKlVi0XVse-w65aMYOtpMqC_69k6YqdMXG19J52fcQcsLZJ854-_maMdY2cmnUB8M_aiGkaMwLsuBqKRrGdPuSLJ4or8mbUn4xxoVi_IgccTNfpViQPzd3qQk4QSyYohupz7tS3VhoGmipGdbVbTFgpCnSHlPFuBtdhUBHXON8uh3kQl0MtK4AM8VYITtfZ7dC77Cunqsm53Oa0gh-M0J5S14Ncxa8e5zH5Pb7t5uzi-bqx_nl2elV42XXmUZ7LV3wnTetUnwJjBmvoBWDkL10sg9t17tOON5qLTTILgyiU11v5ADSaC2PyZeD73rTTxA8xJrdaNcZJ5d3Njm0z5GIK_szbS0XmnOlZoP3jwY5_d5AqXbC4mEcXYS0KVazpRGt2BPVgTh_s5QMw1MIZ3bfm33oze5LsYbbh96smXUn_77wr-pQ1Ix_PeAwr2mLkG3xCNFDwAy-2pDwPwn3R3esZQ</recordid><startdate>19910201</startdate><enddate>19910201</enddate><creator>Darst, S.A.</creator><creator>Ahlers, M.</creator><creator>Meller, P.H.</creator><creator>Kubalek, E.W.</creator><creator>Blankenburg, R.</creator><creator>Ribi, H.O.</creator><creator>Ringsdorf, H.</creator><creator>Kornberg, R.D.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19910201</creationdate><title>Two-dimensional crystals of streptavidin on biotinylated lipid layers and their interactions with biotinylated macromolecules</title><author>Darst, S.A. ; 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| ispartof | Biophysical journal, 1991-02, Vol.59 (2), p.387-396 |
| issn | 0006-3495 1542-0086 |
| language | eng |
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| source | MEDLINE; Cell Press Free Archives; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Bacterial Proteins - chemistry Bacterial Proteins - metabolism Bacterial Proteins - ultrastructure Binding Sites Biotin - metabolism Fluorescein-5-isothiocyanate Fluoresceins Fluorescent Dyes Liposomes Microscopy, Electron Models, Structural Molecular Conformation Protein Binding Protein Conformation Streptavidin Thiocyanates |
| title | Two-dimensional crystals of streptavidin on biotinylated lipid layers and their interactions with biotinylated macromolecules |
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