ABSTRACT
The development of atomic force microscopy (AFM) as a molecular-scale imaging tool that can probe surface processes in situ has enabled researchers to explore some of the physical mechanisms that underlie the control of organic matrices and molecules on mineral nucleation and growth. This chapter presents the topics related to using the tool of in situ AFM to investigate organization of protein matrices that will eventually act as primary templates for subsequent biomineralization processes. It reviews some examples of investigation of self-assembly by different protein systems, illustrates the unique information obtained through in situ AFM imaging, and explains how the analysis of measured quantities is converted into the parameters of scientific interest. The AFM consists of a cantilever with a sharp probe at its end that is used to scan the surface of the specimen. AFM height images of two-dimensional lattice of cowpea mosaic virus, surface of canavalin crystal, and surface of calcium oxalate monohydrate crystal.
