Many vital processes are regulated by the packaging of eukaryotic genomes into nucleosomes and chromatin. The regulation of chromatin requires the precisely orchestrated interplay of  various chromatin-associated proteins. These include  sequence-specific binding factors as well as ATP-dependent chromatin remodeling enzymes (remodelers), which use their ATPase motor to alter the distribution and composition of nucleosomes. In order to understand the mechanisms of these chromatin-associated factors, a quantitative characterization of their complex real-time dynamics is needed. We developed novel fluorescence-based imaging methods that facilitate the study of these processes at the single-molecule level. In this talk, I will describe the new methodology and its applications.