Nor, as many people have assumed, did Max invent the method used to determine those two structures and thousands that have come after them. The method was invented years earlier for small organic molecules by J.M. Robertson of Glasgow University, in a series of brilliant crystallographic studies. Robertson had even suggested at the time that the so-called isomorphous replacement method might be used to solve the structures of very small proteins like insulin. But no one believed it could work for a protein the size of myoglobin, much less hemoglobin, which is four times larger—no one except Max Perutz.
Against the prevailing opinion of nearly every physicist, Max did the experiment. He did it because he had realized that, while the scattering from the thousands of atoms in a protein crystal was weak because the structure was spread out over a large volume, the scattering from a single heavy atom ...