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- W2099885024 abstract "The use of a compact support constraint along the beam direction is considered as a solution to the phase problem for diffraction by two-dimensional protein crystals. Specifically we apply the iterative Gerchberg–Saxton–Fienup algorithm to simulated three-dimensional transmission electron diffraction data from monolayer organic crystals. We find that oversampling along the reciprocal-lattice rods (relrods) normal to the monolayer alone does not solve the phase problem in this geometry in general. However, based on simulations for a crystalline protein monolayer (lysozyme), we find that convergence is obtained in three dimensions if phases are supplied from a few high resolution electron microscope images recorded at small tilts to the beam direction. In the absence of noise, amplitude-weighted phase residuals of around 5°, and a cross-correlation coefficient of 0.96 between the true and estimated potential are obtained if phases are included from images at tilts of up to 15°. The performance is almost as good in the presence of noise at a level that is comparable to that commonly observed in electron crystallography of proteins. The method should greatly reduce the time and labor needed for data acquisition and analysis in cryo-electron microscopy of organic thin crystals by avoiding the need to record images at high tilt angles." @default.
- W2099885024 created "2016-06-24" @default.
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- W2099885024 date "2003-10-01" @default.
- W2099885024 modified "2023-10-16" @default.
- W2099885024 title "Three-dimensional diffractive imaging for crystalline monolayers with one-dimensional compact support" @default.
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- W2099885024 doi "https://doi.org/10.1016/j.jsb.2003.09.019" @default.
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