THE PERFECTION OF PROTEIN CRYSTALS PROBED BY DIRECT RECORDING OF BRAGG REFLECTION PROFILES WITH A QUASI-PLANAR X-RAY WAVE

Profiles of Bragg reflections from earth-grown crystals of lysozyme fr om 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 consi st of only a few (three and two, respectively) highly ordered domains, misoriented with respect to each other by a few are seconds. The smal lest rocking widths were observed for the large domain of the collagen ase sample (FWHM corrected for instrumental broadening: 0.0016 degrees for a strong reflection al 3 Angstrom resolution). With appropriate i mprovements, this method might become a quantitative tool for characte rizing the perfection of crystals from biological macromolecules.