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High-resolution electron crystallography of light-harvesting chlorophyll a/b-protein complex in three different media

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Wang, D. N., & Kühlbrandt, W. (1991). High-resolution electron crystallography of light-harvesting chlorophyll a/b-protein complex in three different media. Journal of Molecular Biology (London), 217(4), 691-9-699. doi:10.1016/0022-2836(91)90526-c.


Cite as: http://hdl.handle.net/21.11116/0000-0007-CBE6-1
Abstract
Large two-dimensional crystals of the light-harvesting chlorophyll a/b-protein complex (LHC-II) from the photosynthetic membrane of pea chloroplasts were grown by a new method from detergent solution. The structure of these crystals was examined by electron crystallography, using three different media to preserve high-resolution detail: vitrified water, glucose and tannin. The crystals diffracted electrons to at least 3.2 A resolution in all three media. R-factors between the three data sets of electron diffraction amplitudes ranged from 6.4% to 14.3%. Fourier difference maps were generated and compared to a projection map of the complex at 3.4 A resolution. No significant differences were found, proving that all three media preserved the native structure of LHC-II at high resolution. The probability of recording high-quality electron diffraction patterns with tannin was 90%. With glucose and water this probability was lower by a factor of 10 to 20, suggesting that tannin may be preferable as a preserving medium for sensitive biological specimens.