Assessment of crystal quality of protein crystals by using rocking curve imaging.

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In the past, the main goal of protein crystallization was to explore the structure of protein molecules using X-ray. Recently, protein crystals have emerged as promising bio-nanoporous materials for different applications including highly selective bio-catalysis, bio-sensing and drug delivery. We identified the dislocation images in the identical protein crystals which are tetragonal hen-egg white lysozyme (HEWL) crystals not only by the conventional film method but the digital method using X-ray CCD camera systems. The simultaneous measurements of both methods were also carried out in the identical HEWL crystals. We evaluate the crystal perfection by mapping angular positions of maximum and the full width of half maximum (FWHM) for the local rocking curves. It is shown that the digital topography is more effective for assessment of crystal quality in protein crystals.