When two become one: Integrating FRET and EPR into one structural model

Abstract

In modern structural biology, rarely one method can provide all structural insights, and integrative approaches combining different results into one framework are the necessary future. For example, cryo-electron microscopy/tomography and x-ray crystallography are well-established techniques yielding atomic-resolution structures of folded proteins. However, these types of structural information may be limited in providing insights on highly dynamic processes or intrinsically disordered proteins. Such data can be complemented by other classes of techniques, such as single-molecule fluorescence resonance energy transfer (smFRET) and electron paramagnetic resonance (EPR) spectroscopy, which measure distances or even distance distributions between labels that can be site-specifically mounted into the biomolecule.