抄録
In situ atomic force microscopy (AFM) was utilized to study growth processes of several macromolecular crystals. Correlation between crystal structure, surface morphology, and growth mechanisms of faces of macromolecular crystals that have screw axes perpendicular to them was demonstrated. Thus the {001} faces of orthorhombic catalase, ribosomal 50 s subunit, trigonal trypsin, and tetragonal Bence-Jones protein (BJP) crystals grow by successive deposition of n alternating, symmetry-related layers with a thickness of d00n＝1/n l c l. For crystallization of glucose isomerase crystals from the supersaturation dependencies of tangential step rates and critical step lengths kinetic coefficient of steps and the free energy of the step edge were estimated respectively. Incorporation of the individual virions into the step edge on the surface o Cucumber Mosaic Virus (CMV) crystals was visualized and attachment frequencies and probabilities were estimated.
