Using DNA as a fiducial marker to study SMC complex interactions with the atomic force microscope.

ABSTRACT: Atomic force microscopy can potentially provide information on protein volumes, shapes, and interactions but is susceptible to variable tip-induced artifacts. In this study, we present an atomic force microscopy approach that can measure volumes of nonglobular polypeptides such as structural maintenance of chromosomes (SMC) proteins, and use it to study the interactions that occur within and between SMC complexes. Together with the protein of interest, we coadsorb a DNA molecule and use it as a fiducial marker to account for tip-induced artifacts that affect both protein and DNA, allowing normalization of protein volumes from images taken on different days and with different tips. This approach significantly reduced the error associated with volume analysis, and allowed determination of th

SUBMITTER: Fuentes-Perez ME 

PROVIDER: S-EPMC3283809 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature