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Synchrotron Small-Angle X-Ray Scattering Investigation on Integral Membrane Protein Light-Harvesting Complex LH2 from Photosynthetic Bacterium Rhodopseudomonas Acidophila |
| DU Lu-Chao1;WENG Yu-Xiang1;HONG Xin-Guo2;XIAN Ding-Chang2;Kobayashi Katsumi3 |
| 1Laboratory of Soft Matter Physics, and Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100080
2Beijing Synchrotron Radiation Facility (BSRF), Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049
3Photon Factory, High Energy Accelerator Research Organization 1-1 Oho, Tsukuba-shi, Ibaraki-ken, 305-0801, Japan |
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| Cite this article: |
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DU Lu-Chao, WENG Yu-Xiang, HONG Xin-Guo et al 2006 Chin. Phys. Lett. 23 1861-1863 |
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Abstract Structures of membrane protein in solution are different from that in crystal phase. We present the primary results of small angle x-ray scattering (SAXS) resolved topological structures of a light harvesting antenna membrane protein complex LH2 from photosynthetic bacteria Rhodopseudomonas acidophila in detergent solution for the first time. Our results show that the elliptical shape of the LH2 complex in solution clearly deviates from its circular structure in crystal phase determined by x-ray diffraction. This result provides an insight into the structure and function interplay in LH2.
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| Keywords:
61.10.Eq
31.15.Ar
87.68.+z
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Published: 01 July 2006
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