A crystal of hen egg-white lysozyme was analyzed by means of energy-dispersive X-ray Laue diffraction with white synchrotron radiation at 2.7 Å resolution using a pnCCD detector. From Laue spots measured in a single exposure of the arbitrarily oriented crystal, the lattice constants of the tetragonal unit cell could be extracted with an accuracy of about 2.5%. Scanning across the sample surface, Laue images with split reflections were recorded at various positions. The corresponding diffraction patterns were generated by two crystalline domains with a tilt of about 1° relative to each other. The obtained results demonstrate the potential of the pnCCD for fast X-ray screening of crystals of macromolecules or proteins prior to conventional X-ray structure analysis. The described experiment can be automatized to quantitatively characterize imperfect single crystals or polycrystals.
Time-dependent X-ray diffraction studies on urea/hen egg white lysozyme complexes reveal structural changes that indicate onset of denaturation
