Abstract
X-ray diffraction experiments were performed to study the effect of forced solution flow on protein-crystal quality. The tetragonal crystals of hen egg white lysozyme were grown under flow in the rate range of 0 (quiescent condition) to 1000 μm/s. The quality of the crystals grown under flow was superior to that of crystals grown under quiescent conditions. To investigate the mechanism of the quality improvement, we observed the surface morphology of the (110) face using atomic force microscopy (AFM). Under quiescent conditions, the two-dimensional (2D) nuclei were randomly formed over the surface. Under solution flow, a hillock consisting of 2D islands was formed around the facet center. The step density under flow was higher than that under quiescent conditions. The step growth rate decreased with increasing flow rate because of the step-density increase. We found that there was a strong correlation between the crystal quality and the step growth rate. The results suggested that the slow growth decreases the molecular misorientation at the kink site, resulting in an improvement in crystal quality.
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