Rocking-curve imaging of high-quality protein crystals by non-dispersive X-ray optics in the double-crystal configuration

Abstract

The double-crystal configuration is useful for the evaluation of strain and defects in single crystals. In this study, rocking curve measurements by X-ray topography in the double-crystal configuration were demonstrated using perfect crystals of the protein glucose isomerase (GI). The setup enables precise evaluation of perfection in protein crystals with the nearly nondispersive X-ray optics. It reveals the uniform perfection of GI crystals according to the theory of X-ray diffraction. It is expected that unknown imperfections in various protein crystals of lower quality will be revealed by the nondispersive configuration using perfect protein crystals.