Abstract
A systematic study of the correlation between supersaturation and protein crystal quality was carried out employing atomic force microscopy (AFM) and X-ray crystallography with synchrotron radiation (SR). The surface morphology and growth rates of hen egg-white (HEW) lysozyme crystals soaked in various supersaturated solutions were first investigated by AFM. The results showed that the formation of two-dimensional islands increased as a function of supersaturation. The growth rate (molecule intake speed) also increased as a function of supersaturation. In order to examine the correlation between the surface morphology, growth rate and the crystal quality, X-ray diffraction experiments were performed. It was confirmed that crystals grown at lower supersaturations diffracted better with higher signal-to-noise ratios, including better agreement between symmetry-related reflections. The results strongly suggested that the molecular misorientation at high supersaturation affected the crystal quality.
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Schedule a callMore From: Acta Crystallographica Section D Biological Crystallography
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