Synchrotron small-angle X-ray scattering investigation on integral membrane protein light-harvesting complex LH2 from photosynthetic bacterium rhodopseudomonas acidophila

被引：8

作者：

Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100080, China ^{[1
]}

不详 ^{[2
]}

不详 ^{[3
]}

不详 ^{[4
]}

机构：

[1] Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences

[2] Beijing Synchrotron Radiation Facility (BSRF), Institute of High Energy Physics, Chinese Academy of Sciences

[3] Photon Factory, High Energy Accelerator Research Organization, Tsukuba-shi, Ibaraki-ken, 305-0801

[4] Argonne National Laboratory, GSECARS, Consortium for Advanced Radiation Sources, Argonne, IL 60439

来源：

Chin. Phys. Lett. | 2006年 / 7卷 / 1861-1863期

关键词：

X ray diffraction;

D O I：

10.1088/0256-307X/23/7/057

中图分类号：

学科分类号：

摘要：

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. © 2006 Chinese Physical Society and IOP Publishing Ltd.

引用

页码：1861 / 1863

页数：2

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