Isolating functional units from large insoluble protein complexes are a complex but valuable approach for quantitative and structural analysis. Mycoplasma mobile, a gliding bacterium, contains a large insoluble protein complex called gliding machinery. The machinery contains several chain structures formed by motors that are evolutionarily related to the F-ATPase. Recently, we developed a method to purify functional motors and their chain structures using Triton X-100 and a high salt concentration buffer and resolved their structures using electron microscopy. In this chapter, we describe the processes of purification and structural analysis of functional motors for the gliding of M. mobile using negative-staining electron microscopy.
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