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在磷的K吸收边附近波长处的X射线光谱学和X射线衍射

X-ray spectroscopy and X-ray diffraction at wavelengths near the K-absorption edge of phosphorus.

作者信息

Biou Valérie, Bösecke Peter, Bois Jean Marie, Brandolin Gérard, Kahn Richard, Mas Corinne, Nauton Lionel, Nury Hugues, Pebay-Peyroula Eva, Vicat Jean, Stuhrmann Heinrich

机构信息

Laboratoire d'Enzymologie et de Biochimie Structurales CNRS, Avenue de la Terrasse, 91198 Gif sur Yvette CEDEX, France.

出版信息

J Synchrotron Radiat. 2005 Jul;12(Pt 4):402-9. doi: 10.1107/S0909049505009222. Epub 2005 Jun 15.

Abstract

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.

摘要

磷是生物体内一种丰富的元素。通过其X射线吸收光谱可对其进行追踪,该光谱在其K边缘显示出一条强烈的白线,这与稀土离子L(III)边缘所观察到的情况类似。对于紫膜,发现磷反常色散虚部的变化接近20个反常电子单位。在磷的K吸收边缘附近波长处进行的反常衍射实验证实了这一结果。由反常衍射得出的脂质空间分布与早期中子衍射结果一致。使用5.76埃光子对载体蛋白单晶进行的测试实验给出了首个低分辨率衍射图样。尝试了各种晶体安装技术。此外,对苏氨酸合酶溶液进行的荧光测量似乎暗示,激活剂结合后辅因子的磷酸盐环境发生了变化。

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