SCSB Report

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چکیده

ollaborations with the MXL utilizing Small Angle X-ray Scattering (SAXS) have yielded new insight about the proteins being studied. While crystallization results in a static picture of a single conformation of your protein, and NMR is generally restricted to a single molecule of limited size, in solution your molecule may adopt one, two, or several conformations. Cryo-EM offers one method of imaging samples in solution, Small Angle X-ray Scattering (SAXS) provides another complementary method. In the last several years analysis tools for SAXS data have grown to include tools for querying ensembles of structures to find those that best match the solution scattering profile. Some programs that do this are: MES (Hammel), EOM (Svergun), and McSAS (Pauw). While EOM and MES require a model of your sample, and an idea of its flexibility, McSAS (MonteCarlo-SAS) is an ab initio method which determines the equivalent distribution of spheres (DOS) that matches the scattering from your sample. This can be very helpful in those cases where the structure or assembly is unknown, as in the case of protein fibril formation. In the case of subtle differences, small changes in scattering properties can also be very revealing. Hura et al. Recently promoted the use of correlation coefficients in analyzing SAXS data from multiple samples. In a similar analysis we utilized the cross-X value to determine that the effect of a known activating point mutation on the shape of our target protein was identical to that of the activating ligand. C

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تاریخ انتشار 2013