Figure 1

SAXS analysis of Pae χψ and Pae χψ _(Δ1-85) . ( A ) Pair-distribution functions (normalized to equal peak height) of Pae χψ (blue) and Pae χψ_(Δ1-85) (red) calculated with GNOM indicate that Pae χψ is more elongated than Pae χψ_(Δ1-85). ( B ) Radius of gyration distributions of pools (black line) and selected structures (red area) for the EOM analysis of full-length Pae χψ. ( C ) Ab initio shape of Pae χψ_(Δ1-85) (transparent red) calculated with GASBOR with the modeled Eco χPae ψ-structure (see text) docked into the density. ( D ) Superposition of the selected structures from EOM analysis of full-length Pae χψ. The structures were superimposed using only the core-domains of the proteins (shown in grey for simplification of the image). The flexible N-terminal residues of Paeψ are shown in a different color for each of the selected structures. SAXS experiments were performed in 20 mM Hepes pH 7.4, 50 mM NaCl, 3% (w/v) sucrose, 1 mM NaN₃, 1 mM DTT.