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• W2067020293 abstract "Thin, three-dimensional crystals of CaATPase have been studied at high resolution by electron crystallography. These crystals were grown by adding purified CaATPase to appropriate concentrations of lipid, detergent and calcium. A thin film of crystals was then rapidly frozen and maintained in the frozen-hydrated state during electron microscopy. The resulting electron diffraction patterns extend to 4.1 A resolution and images contain phase data to 6 A resolution. By combining Fourier amplitudes from electron diffraction patterns with phases from images, a density map has been calculated in projection. Comparison of this map from unstained crystals with a previously determined map from negatively stained crystals reveals distinct contributions from intramembranous and extramembranous protein domains. On the basis of this distinction and of the packing of molecules in the crystal, we have proposed a specific arrangement for the ten alpha-helices that have been suggested as spanning the bilayer." @default.
• W2067020293 created "2016-06-24" @default.
• W2067020293 creator A5006337666 @default.
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• W2067020293 date "1990-06-01" @default.
• W2067020293 modified "2023-10-15" @default.
• W2067020293 title "Structure of CaATPase: Electron microscopy of frozen-hydrated crystals at 6 Å resolution in projection" @default.
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• W2067020293 doi "https://doi.org/10.1016/s0022-2836(05)80213-x" @default.
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