Abstract
The separation of two conformational states of 3-isopropylmalate dehydrogenase molecules from Thermus thermophilus in solution on a gel chromatographic column, attached to a sample cell of a small-angle X-ray scattering synchrotron beamline, has been simulated. The scattering intensity profiles from the open and closed forms of the enzyme molecules were restored by evolving factor analysis (EFA) using the synthetic data set with added Poisson noise at the relative level of 3–5%. Thus, the efficiency of the EFA algorithm is confirmed in the case of two-component mixtures consisting of particles with the same molecular masses.
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