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Three-dimensional crystals of an integral membrane protein: an initial x-ray analysis
Matrix protein, a pore-forming transmembrane protein spanning the outer membrane of Escherichia coli, has been obtained in a variety of three- dimensional crystal forms amenable to both electron microscope and x- ray analyses. Successful association into large crystals depended on the use of alpha-o...
| Formato: | Texto |
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| Lenguaje: | English |
| Publicado: |
The Rockefeller University Press
1980
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| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110650/ https://www.ncbi.nlm.nih.gov/pubmed/6252213 |
| _version_ | 1782139633658757120 |
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| collection | PubMed |
| description | Matrix protein, a pore-forming transmembrane protein spanning the outer membrane of Escherichia coli, has been obtained in a variety of three- dimensional crystal forms amenable to both electron microscope and x- ray analyses. Successful association into large crystals depended on the use of alpha-octyl glucoside, a detergent with relatively low affinity for the protein. Electron micrographs of thin-sectioned crystals show a high degree of order. Preliminary crystallographic data suggest that the crystals, which exhibit diffraction to 3.8 A, have a cubic space group. |
| format | Text |
| id | pubmed-2110650 |
| institution | National Center for Biotechnology Information |
| language | English |
| publishDate | 1980 |
| publisher | The Rockefeller University Press |
| record_format | MEDLINE/PubMed |
| spelling | pubmed-21106502008-05-01 Three-dimensional crystals of an integral membrane protein: an initial x-ray analysis J Cell Biol Articles Matrix protein, a pore-forming transmembrane protein spanning the outer membrane of Escherichia coli, has been obtained in a variety of three- dimensional crystal forms amenable to both electron microscope and x- ray analyses. Successful association into large crystals depended on the use of alpha-octyl glucoside, a detergent with relatively low affinity for the protein. Electron micrographs of thin-sectioned crystals show a high degree of order. Preliminary crystallographic data suggest that the crystals, which exhibit diffraction to 3.8 A, have a cubic space group. The Rockefeller University Press 1980-07-01 /pmc/articles/PMC2110650/ /pubmed/6252213 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
| spellingShingle | Articles Three-dimensional crystals of an integral membrane protein: an initial x-ray analysis |
| title | Three-dimensional crystals of an integral membrane protein: an initial x-ray analysis |
| title_full | Three-dimensional crystals of an integral membrane protein: an initial x-ray analysis |
| title_fullStr | Three-dimensional crystals of an integral membrane protein: an initial x-ray analysis |
| title_full_unstemmed | Three-dimensional crystals of an integral membrane protein: an initial x-ray analysis |
| title_short | Three-dimensional crystals of an integral membrane protein: an initial x-ray analysis |
| title_sort | three-dimensional crystals of an integral membrane protein: an initial x-ray analysis |
| topic | Articles |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110650/ https://www.ncbi.nlm.nih.gov/pubmed/6252213 |