Abstract
In order to determine the molecular structure by x-ray diffraction analysis, it is very important to grow high quality protein crystals. The molecular resolution imaging of soluble protein crystals such as the tetragonal lysozyme (110) face in saturated solution is demonstrated using frequency-modulation atomic force microscopy (FM-AFM). The surface structure of the (110) face and the crystallographic position of individual molecules were determined from molecular resolution images. For observation of protein crystals, FM-AFM is a favorable technique as an alternative to contact mode or amplitude-modulation AFM.
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