Abstract
We have developed a new methodology that determines protein structures using Small-angle X-ray scattering (SAXS) data. The current bottlenecks in determining the protein structures require a new strategy using the simple design of an experiment, and SAXS is suitable for this purpose in spite of its low information content. We performed structure calculations using the SAXS constraints combined with various types of structural information. The result shows that the SAXS constraints complement the tertiary structure for the proteins, and furthermore, a coarse-grained protein structures at the residue resolution can be constructed from only the SAXS data and the information about the secondary structure.
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