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- W1986228082 abstract "Protein X-ray crystallography is a method for determining the 3-dimensional structures of large biological molecules arranged in regular arrays inside a crystal. Samples of the Fourier magnitude of the molecular charge density can be measured from the amplitudes of the scattered X-rays but the determination of the Fourier phases requires chemical modification to the sample and collection of additional data. There is thus a need for a direct digital phasing method that does not require modified specimens. The diffraction from very small crystals allows for a finer sampling of the diffraction amplitude and although highly attenuated, these additional samples offer the possibility of iterative phase retrieval without the use of ancillary experimental data. Following on from a previous study [6], we examine in detail the noise characteristics of finite crystal diffraction and propose a data selection strategy to improve 3-dimensional reconstructions of the molecular charge density using iterative phase retrieval algorithms. Simulation results verify that higher noise levels can indeed be tolerated by employing such a strategy to precondition the data." @default.
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- W1986228082 date "2012-11-26" @default.
- W1986228082 modified "2023-09-27" @default.
- W1986228082 title "Phase retrieval in femtosecond x-ray nanocrystallography" @default.
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- W1986228082 doi "https://doi.org/10.1145/2425836.2425847" @default.
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