Abstract
The small‐angle scattering function of hemoglobin for X‐rays and neutrons has been calculated from the atomic coordinates of hemoglobin, established by X‐ray diffraction analysis. These theoretical scattering functions were compared with the experimental scattering data on aqueous hemoglobin solutions reported previously. The good agreement of the two sets of data in and beyond the region of the Guinier approximation gives confidence to the statement that the three‐dimensional structures of hemoglobin in single crystal and in aqueous solution are the same.
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