At its birth, witnessed by the structure determination of myoglobin and hemoglobin and by the Watson and Crick model of B-DNA, structural biology was essentially a single-technique discipline focused around X-ray crystallography. Indeed, it took almost three decades before NMR spectroscopy introduced itself as a significant technique for macromolecular structure determination. In contrast, modern structural biology in 2011 is an interdisciplinary field, which integrates detailed structural information obtained from X-ray crystallography and NMR with low resolution information from complementary sources such as electron microscopy, SAXS, light scatter and general biophysics techniques.
SBB and L-PROBE tackle a wide variety of structural biology problems using such a broad multi-disciplinary approach. Next to the detailed structure determination by NMR and X-ray crystallography, we complement our experimental platform with low resolution techniques, and in particular SAXS and MALS. SAXS has the advantage to provide relevant and specific structural information for those proteins or regions within proteins where the two classic techniques fail completely. MALS is complimentary to this and an essential in sample preparation.