Abstract
Profiles of Bragg reflections from earth-grown crystals of lysozyme from hen egg-white and collagenase from Hypoderma lineatum were directly recorded with a quasi-planar X-ray wave. One crystal of each protein was chosen for a detailed investigation. Each sample is shown to consist of only a few (three and two, respectively) highly ordered domains, misoriented with respect to each other by a few arc s. The smallest rocking widths were observed for the large domain of the collagenase sample (FWHM corrected for instrumental broadening: 0.0016 degrees for a strong reflection at 3 A resolution). With appropriate improvements, this method might become a quantitative tool for characterizing the perfection of crystals from biological macromolecules.
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