Yang J, Tamm L K, Tillack T W, Shao Z
Bio-SPM Laboratory, University of Virginia, Charlottesville 22908.
J Mol Biol. 1993 Jan 20;229(2):286-90. doi: 10.1006/jmbi.1993.1033.
We demonstrate that supported synthetic phospholipid bilayers, which are stabilized by lateral cross-linking in both leaflets, can be used for specimen preparation for atomic force microscopy of purified membrane proteins with high stability and excellent reproducibility under water or low-salt buffer. A bilayer containing 1,2-dipentacosa-10,12-diynoyl-phosphatidylcholine and 20 mol % ganglioside (GM1) was transferred onto the surface of mica from a Langmuir trough. Cholera toxin, both the B-subunit and the complete molecular randomly bound to the gangliosides, were imaged by atomic force microscopy in solution with a resolution of better than 2 nm. The pentameric structure of the B-subunit oligomers was well resolved. This result indicates that, with this preparation procedure, other membrane proteins may be studied at intermediate to high resolution under physiologically relevant conditions without the need for crystallization.
我们证明,通过在两个小叶中进行横向交联而稳定的负载型合成磷脂双层,可用于在水或低盐缓冲液中以高稳定性和出色的重现性对纯化的膜蛋白进行原子力显微镜检查的样品制备。将含有1,2-二戊五碳-10,12-二炔酰基磷脂酰胆碱和20 mol%神经节苷脂(GM1)的双层从Langmuir槽转移到云母表面。霍乱毒素的B亚基和完整分子随机结合到神经节苷脂上,通过原子力显微镜在溶液中成像,分辨率优于2 nm。B亚基寡聚体的五聚体结构得到了很好的解析。该结果表明,通过这种制备方法,可以在生理相关条件下以中高分辨率研究其他膜蛋白,而无需结晶。