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- W2160705239 abstract "With careful experimental design, indexed synchrotron white-beam X-ray topographs of ribonuclease S crystals at ambient temperature could be recorded with a definition and contrast comparable to that of monochromatic beam topographs of other proteins reported in the literature. By excluding wavelengths longer than 1 Å from the white beam with a filter, a radiation dose equivalent to that required to record about 18 topographs could be tolerated without appreciable radiation damage to the samples. Bragg angles of 0.5° or less were required to select low-index harmonically pure reflections with high intensities and extinction lengths only several times the sample's thickness. The resulting X-ray topographs in some cases showed topographic detail and in others showed the even featureless background that has been considered characteristic of a protein crystal of low mosaicity. The ribonuclease S crystals were well ordered single crystals of a quality comparable to other protein crystals that have been studied by X-ray topography." @default.
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- W2160705239 date "2002-03-22" @default.
- W2160705239 modified "2023-10-16" @default.
- W2160705239 title "Synchrotron white-beam X-ray topography of ribonuclease S crystals" @default.
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- W2160705239 doi "https://doi.org/10.1107/s090744490200121x" @default.
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