The single-stranded DNA binding protein (SSB) plays a fundamental role in DNA metabolism, including replication, recombination, and repair. The main target of our investigations, E.coli SSB (EcSSB) is the prototype of tetrameric SSB-s. EcSSB contains a globular oligonucleotide-binding (OB) domain (1-112) and an intrinsically disordered C-domain (113-177) which acts as a flexible hub recruiting partner proteins and establishes the propensity of EcSSB to undergo liquid-liquid phase separation (LLPS). LLPS condensates of EcSSB form as dynamic, membraneless organizing hubs which play crucial role in the genome maintenance processes. To characterize the physicochemical properties of such EcSSB condensates and the underlying weak interactions we use solution state NMR spectroscopy which provides non-invasive structure determination at atomic resolution and experimental conditions close to the physiological state.