Synchrotron white-beam X-ray topography of ribonuclease S crystals.

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. [ABSTRACT FROM AUTHOR]