Abstract
The determination of membrane protein structures at high-resolution requires crystallographic methods. Progress with x-ray crystallography of three-dimensional (3D) crystals has been less rapid than was hoped 10 years ago. However, electron microscopy and electron diffraction of two-dimensional (2D) crystals now offers a viable alternative. The 3D structures of three membrane proteins, namely bacteriorhodopsin (Henderson et al, 1990), PhoE porin (Jap et al, 1991) and plant light-harvesting complex (Kühlbrandt & Wang, 1991), have to date been determined by this method at resolutions ranging from 3.5 to 6Å.
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© 1992 Springer Science+Business Media Dordrecht
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Kühlbrandt, W. (1992). High-Resolution Electron Microscopy of Membrane Proteins. In: Pullman, A., Jortner, J., Pullman, B. (eds) Membrane Proteins: Structures, Interactions and Models. The Jerusalem Symposia on Quantum Chemistry and Biochemistry, vol 25. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-2718-9_2
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DOI: https://doi.org/10.1007/978-94-011-2718-9_2
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