journal menu
![[Figure 3]](ni5011fig3mag.jpg)
|
|
Figure 3
VanRSc oligomerizes in the presence of beryllium fluoride. (a) Sedimentation-velocity analytical ultracentrifugation. Experimental data are shown as circles and fits of the Lamm equation are shown as lines; residuals from the fit are shown below the data panels. Only every third boundary and third data point are shown for clarity. Measurements were performed at a 36.5 µM monomer concentration at 20°C. (b) c(s) distributions derived from the fitting of the Lamm equation to the data shown in (a), as implemented in SEDFIT. The overall r.m.s.d. is 0.005 Å for both fits. This analysis shows evidence of monomer plus small amounts of a larger species in the absence of ![[{\rm BeF}_{3}^{-}]](teximages/ni5011fi2.svg) , and monomers, dimers and tetramers in the presence of . These observations are consistent with the association constants derived from direct fitting of the sedimentation-velocity data to association models (see Supplementary Fig. S3 and Supplementary Table S3). (c) Sedimentation-equilibrium analytical ultracentrifugation. Representative data for 16.7 µM protein in the absence of (left) and for 47.3 µM protein in the presence of (right) are shown. Model fits are shown as lines for each of three radial absorbance boundaries collected at three speeds (18 000, 20 000 and 22 000 rev min−1); residuals for the model fitting are shown below the data panels. Data collected in the absence of are best described by a weak monomer–dimer equilibrium model consistent with the two species observed by sedimentation velocity; data collected in the presence of are best described by a monomer–dimer–tetramer equilibrium. Fit parameters are shown in Supplementary Table S4. Figures were prepared using GUSSI. |
![[Figure 3]](ni5011fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
Open 
access
access
