Figure 2
(a) The self-rotation function for B.c TssA CTD crystals calculated on all data from 55.90 to 3.79 Å resolution using a 44 Å radius of integration. The section shown corresponds to κ = 180°, with the orthogonal x, y and z axes along the crystallographic a, b and c axes, respectively. Noncrystallographic twofold axes can be seen every 11.25° in the bc plane at approximately 70% of the origin. The image was generated in POLARRFN (Winn et al., 2011). (b) Gel-filtration chromatogram of B.c SeMet-MBP-TssA CTD protein, with UV absorption (280 nm) shown as a dotted blue line and the elution volume (70.77 ml) corresponding to B.c TssA CTD shown above the curve. Inset: calibration curve for the gel-filtration column, with Kav = 0.4 (Ve = 70.77 ml) highlighted corresponding to a molecular mass of ∼3.55 × 105 Da for B.c TssA CTD. |