Journal: bioRxiv

Article Title: Solution structure of human STARD1 protein and its interaction with fluorescently-labeled cholesterol analogues with different position of the NBD-group

doi: 10.1101/116368

Figure Lengend Snippet: Analysis of hydrodynamics and solution structure of STARD1 S195E by SAXS coupled to SEC. A. SEC profile of STARD1 S195E followed by triple detection Malvern system (absorbance at 280 nm (Abs, blue), refractive index (RI, red), right angle light scattering (RALS, green) and synchrotron SAXS at 20 °C. Note that the flow was split for simultaneous Malvern and SAXS detection, which is reflected by a doubly reduced elution volume. Molecular weight distribution determined from RALS data and calibration by BSA run is shown by black line. B. The final SAXS curve produced by scaling and averaging frames corresponding to the maximum of the peak from panel A. Guinier region is shown in the inset. C. Dimensionless Kratky plot showing the compactness/rigidity of STARD1 S195E compared to the theoretical curve for a rigid sphere (black dashed line). D. Superposition of the average ab initio molecular envelope generated by DAMMIF/DAMAVER and the modified crystal structure of STARD1 (see text) providing the fit shown by red curve in panels B and C ( model 1 ). The main features of the STARD1 structure are indicated. Drawn using PyMol 1.69 and Chimera 1.11. STARD1 model was superposed with the molecular envelope using “fit to map” tool in Chimera.

Article Snippet: Protein concentration was determined using Bradford microassay [ ] and calibration curve build by BSA standard solutions (ThermoFischer Scientific Inc.).

Techniques: Molecular Weight, Produced, Generated, Modification