Figure 6

The form of TR-His-TMV-CP19 proteins were analyzed by SEC and 17% Native-PAGE and the diffraction analysis of crystals on proteins of TR-His-TMV-CP19 and WT-His-TMV-CP12 (A) The assembly of TR-His-TMV-CP19 was measured by Superdex 200 10/300 GL Column, Blue line represented TR-His-TMV-CP19 dialyzed against 0.2 mol/L ammonium sulfate and 0.1 mol/L Tris solution ( PH 8.0 ) at room temperature for 12 hr. Protein peaks were monitored by UV absorbance at wavelength of 280 nm and retention volumes corresponding to molecular mass were recorded in 20 mM PB and 100 mM sodium chloride, the molecular mass standards were indicated on top of the figure;Red line represents TMV-CP control which did not dialyze against, (B) the 17% Native-PAGE of WT-His-TMV-CP19. As shown in lane M. Numbers on the left were the MW of the standards in kDa, Lanes 1, 2, correspond to the WT-His-TMV-CP19 dialyzed against 0.2 mol/L ammonium sulfate and 0.1 mol/L Tris solution ( PH 8.0 ) at room temperature for 12 hr, (C) the 17% Native-PAGE of WT-His-TMV-CP19. As shown in lane M. Numbers on the left were the MW of the standards in kDa, Lanes 1, 2, correspond to the WT-His-TMV-CP19 did not dialyze against the corresponding solution, (D) X-ray crystal diffraction of WT-His-TMV-CP12 marked in Figure 5B, (E) X-ray crystal diffraction of TR-His-TMV-CP19 marked in Figure 6A, (F) X-ray crystal diffraction of TR-His-TMV-CP19 marked in Figure 6G, (G) X-ray crystal diffraction of TR-His-TMV-CP19 marked in Figure 6J, (H) X-ray crystal diffraction of TR-His-TMV-CP19 obtained from the conditions of Figure 6J, (I) The Four-layer aggregate structure of TR-His-TMV-CP19 incorporated His-tags.