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The use of small-angle X-ray solution scattering (SAXS) as an analytical chemical tool for structural molecular biology is a mature field dating back to the work of Glatter and Kratky in the 1950s. 1 At that time, X-ray tube sources were used and it could take many hours or even days to collect a useful smallangle scattering profile of a protein in solution. The development of synchrotron radiation sources from multi-GeV electron and positron storage rings increased the available flux on the sample by factors of more than 105. Use of these sources coupled with electronic detectors made it possible to start collecting useful SAXS data on much more rapid time scales, which can now go down to tens of milliseconds and in special cases even faster than a millisecond. Despite these enormous advances in data acquisition for SAXS, use of the technique in structural molecular biology has been relatively slow in developing …