Abstract
Solution small angle X-ray scattering (SAXS) was used to confirm the oligomeric state of several structural genomics protein targets from the New York Structural GenomiX Research Consortium. The oligomeric state is representative of the natively active form of the protein and it was determined to corroborate the Protein Data Bank (PDB) structure of a clone or related protein. PDBs are usually modeled from X-ray crystallography and the results of crystalline structures are not often representative of the correct biological assembly. Therefore, the analysis done here was essential to find the natural form. Using solution SAXS allowed us to look at each protein in its native state dissolved in a solution, rather than placed into a crystal array where it is unknown if interactions between each molecule are forced or natural. After obtaining a scattering pattern, several software programs from the ATSAS program suite for small-angle scattering data analysis were utilized to distinguish the quaternary structures of the proteins from monomers to tetramers. The final products were low-resolution three-dimensional structures accurate to the native form of the proteins.