Supplementary Figure 2: SAXS measurements of MtSnf2.
From: Structure of chromatin remodeler Swi2/Snf2 in the resting state
(a) Three different views of the overlay of the final average ab initio molecular envelope of MtSnf2 (445-1176) reconstructed from SAXS measurements (grey) with the docked crystal structure. The protein is colored as in Fig.1, and the N-and C-termini are labeled. Additional densities near the N- and C-termini can be attributed to the disordered residues at both ends (the first 13 and the last 48 residues, respectively). (b) Scattering intensity in arbitrary units versus momentum transfer q in Å-1 for MtSnf2. The linear fitting in the Guinier region of scattering curve (inset) indicates that MtSnf2 is monodisperse and homogenuous in solution. (b) The dimensionless Kratkyplot of MtSnf2 has typical feature for folded protein with disordered regions. (d) Pair distance distribution function (PDDF) of MtSnf2 with Dmax= 117 Å calculated using GNOM (qmax=0.30 Å-1). (e) Fitting the theoretical scattering curve (red line) of MtSnf2 crystal structure to the experimental scattering curve (black circles), with a chi of 2.1. The theoretical SAXS curve agrees well with the SAXS measurement in solution, further validating the observed conformation in the crystals.
