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• W2079718938 abstract "Large two-dimensional crystals of the light-harvesting chlorophyll ab-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 Å 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 Å 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." @default.
• W2079718938 created "2016-06-24" @default.
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• W2079718938 creator A5056113892 @default.
• W2079718938 date "1991-02-01" @default.
• W2079718938 modified "2023-10-15" @default.
• W2079718938 title "High-resolution electron crystallography of light-harvesting chlorophyll -protein complex in three different media" @default.
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• W2079718938 doi "https://doi.org/10.1016/0022-2836(91)90526-c" @default.
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