Two-dimensional crystallization technique for imaging macromolecules, with application to antigen-antibody-complement complexes
Two-dimensional crystals are formed from macromolecules bound on the surface of a lipid monolayer. A ligand linked to the lipid orientates the binding, and lateral diffusion of the lipids facilitates crystallization. The crystals are suitable for structural analysis by image processing of electron m...
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| Veröffentlicht in: | Nature (London) 1983-01, Vol.301 (5896), p.125-129 |
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| container_end_page | 129 |
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| container_issue | 5896 |
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| container_title | Nature (London) |
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| creator | Uzgiris, Egidijus E Kornberg, Roger D |
| description | Two-dimensional crystals are formed from macromolecules bound on the surface of a lipid monolayer. A ligand linked to the lipid orientates the binding, and lateral diffusion of the lipids facilitates crystallization. The crystals are suitable for structural analysis by image processing of electron micrographs. An example is the formation of ordered arrays of antibodies on a monolayer of a lipid hapten, and subsequent decoration of these arrays with the first component of complement. Image processing indicates the arrangement of antibodies and the site of complement binding. This approach should be widely applicable to molecular complexes, such as those in replication, protein synthesis, hormone–receptor interaction and metabolic processes. |
| doi_str_mv | 10.1038/301125a0 |
| format | Article |
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A ligand linked to the lipid orientates the binding, and lateral diffusion of the lipids facilitates crystallization. The crystals are suitable for structural analysis by image processing of electron micrographs. An example is the formation of ordered arrays of antibodies on a monolayer of a lipid hapten, and subsequent decoration of these arrays with the first component of complement. Image processing indicates the arrangement of antibodies and the site of complement binding. This approach should be widely applicable to molecular complexes, such as those in replication, protein synthesis, hormone–receptor interaction and metabolic processes.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/301125a0</identifier><identifier>PMID: 6823289</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Antigen-Antibody Complex ; Biological and medical sciences ; Complement System Proteins - immunology ; Crystalline structure ; Crystallization ; Fundamental and applied biological sciences. 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Psychology</subject><subject>Humanities and Social Sciences</subject><subject>Macromolecular Substances</subject><subject>Methods</subject><subject>Microscopy, Electron</subject><subject>Molecular biophysics</subject><subject>multidisciplinary</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Structure in molecular biology</subject><subject>X-Ray Diffraction</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU-L1TAUxYMo45tR8AsoWYgoWE3apkmXMox_YMDNuC5JevMmQ5rUJGXmufGrm0frWwluckPOL-dy70HoBSUfKGnEx4ZQWjNJHqEdbXlXtZ3gj9GOkFpURDTdU3Se0h0hhFHenqGzTtRNLfod-n1zH6rRTuCTDV46rOMhZemc_SVzecEZ9K23PxfAJkRsJ7m3fo8nqWOYggO9OEjv8b3Nt1jOs7N6-xaw9NnuwVfHqsJ4qHSYZgelVcbr9QHSM_TESJfg-VYv0I_PVzeXX6vr71--XX66rnTTs1xxCrUEDaMB0dSaKUKhNZwr0SkJlJWZqarHVpWzNUYrI40ZVT-qkRtheHOB3qy-cwxlmJSHySYNzkkPYUmDIA0ThPX_BSljHemEKODbFSybSCmCGeZY1hMPAyXDMZThbygFfbl5LmqC8QRuKRT99abLpKUzUXpt0wnrW94zesTerVgqit9DHO7CEkto6V8tX62sl3mJcPI6AX8AofSv_Q</recordid><startdate>19830113</startdate><enddate>19830113</enddate><creator>Uzgiris, Egidijus E</creator><creator>Kornberg, Roger D</creator><general>Nature Publishing Group UK</general><general>Nature Publishing</general><scope>IQODW</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>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19830113</creationdate><title>Two-dimensional crystallization technique for imaging macromolecules, with application to antigen-antibody-complement complexes</title><author>Uzgiris, Egidijus E ; Kornberg, Roger D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c395t-71e2aecedfe832c5b01e4f77b86bae154761b2d4b1b24ffcbfaffdb9dbd7f8f73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Antigen-Antibody Complex</topic><topic>Biological and medical sciences</topic><topic>Complement System Proteins - immunology</topic><topic>Crystalline structure</topic><topic>Crystallization</topic><topic>Fundamental and applied biological sciences. 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| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 1983-01, Vol.301 (5896), p.125-129 |
| issn | 0028-0836 1476-4687 |
| language | eng |
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| source | MEDLINE; Nature; Alma/SFX Local Collection |
| subjects | Antigen-Antibody Complex Biological and medical sciences Complement System Proteins - immunology Crystalline structure Crystallization Fundamental and applied biological sciences. Psychology Humanities and Social Sciences Macromolecular Substances Methods Microscopy, Electron Molecular biophysics multidisciplinary Science Science (multidisciplinary) Structure in molecular biology X-Ray Diffraction |
| title | Two-dimensional crystallization technique for imaging macromolecules, with application to antigen-antibody-complement complexes |
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