Structural dynamics of human FACT protein complex: electron microscopy analysis

Identification of the NTD in hFACT Complex by Electron Microscopy

“…In summary, here we identified and localized SPT16-NTD domain of human FACT for first time. This localization is in a good agreement with previously proposed one based on confirmation flexibility of hFACT [9]. During the act of the conformational change the flexible SPT16 N-terminal domain (NTD) moves away from the other subunits and therefore is not resolved in more open conformational states of hFACT, while less mobile DDs and MDs maintain more compact structure.…”

“…Previously we have shown that nucleosome-free hFACT is a dynamic structure taking "closed" and "open" states [9]. Based on 2D-classes comparison we see complete hFACT in compact "closed" conformation that is characterized by four domains (Figure 1A), while SPT16NTD truncated mutant in the compact state lacks one of the four densities (Figure 1B).…”