X-ray spectroscopy and X-ray diffraction at wavelengths near the K-absorption edge of phosphorus
Phosphorus is an abundant element in living organisms. It is traceable by its X-ray absorption spectrum which shows a strong white line at its K-edge, comparable with that observed for the L(III) edges of rare earth ions. With purple membrane, the variation of the imaginary part of the anomalous dis...
| Publié dans: | Journal of synchrotron radiation. - 1994. - 12(2005), Pt 4 vom: 21. Juli, Seite 402-9 |
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| Auteur principal: | |
| Autres auteurs: | , , , , , , , , , |
| Format: | Article |
| Langue: | English |
| Publié: |
2005
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| Accès à la collection: | Journal of synchrotron radiation |
| Sujets: | Evaluation Study Journal Article Phosphorus 27YLU75U4W Mitochondrial ADP, ATP Translocases 9068-80-8 Carbon-Oxygen Lyases EC 4.2.- threonine synthase EC 4.2.3.1 |
| Résumé: | Phosphorus is an abundant element in living organisms. It is traceable by its X-ray absorption spectrum which shows a strong white line at its K-edge, comparable with that observed for the L(III) edges of rare earth ions. With purple membrane, the variation of the imaginary part of the anomalous dispersion of phosphorus is found to be close to 20 anomalous electron units. Anomalous diffraction experiments at wavelengths near the K-absorption edge of phosphorus confirm this result. The spatial distribution of lipids derived from anomalous diffraction agrees with earlier results from neutron diffraction. Test experiments on single crystals of the carrier protein using 5.76 A photons gave a first low-resolution diffraction pattern. Various techniques of crystal mounting were attempted. In addition, fluorescence measurements on a solution of threonine synthase appear to hint at a change of the phosphate environment of the cofactor upon activator binding |
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| Description: | Date Completed 23.08.2005 Date Revised 10.12.2019 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1600-5775 |