Protein Shape Determination by Small Angle X-Ray Scattering

The 3-dimensional shape of Glucose Isomerase in solution was studied by using a laboratory small-angle X-ray scattering system. The solution structure of this protein obtained by SAXS is in good agreement with the structure obtained by X-ray crystallography.

SAXS and proteins in solution

Commonly used methods for structure analysis of biological macromolecules are single-crystal X-ray diffraction (SC-XRD) and nuclear magnetic resonance spectroscopy (NMR). Both methods can determine the atomic structure of the biological macromolecules.

Small-angle X-ray scattering (SAXS) complements both these high-resolution techniques with valuable additional information and offers specific benefits compared to crystallography: SAXS allows obtaining the 3-dimensional structure of proteins and protein assemblies in solution which is essential for a better understanding of their biological function.

The low resolution 3D structure based on X-ray scat-tering data, calculated by ab-initio methods1, is indis-pensable additional information to the high resolution structures of protein samples provided by SC-XRD and NMR techniques.

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