Background

X-ray crystallography is a fundamental technique for obtaining atomic resolution structural information about macromolecules. However, the requirement for diffraction quality crystals often limits its efficacy for studying protein complexes or systems with inherent structural disorder. In cases where crystallographic methods fall short, small angle X-ray scattering (SAXS) provides a complementary tool for extracting structural information from biological systems. In particular, SAXS proves ideal for studying partially disordered macromolecules, for monitoring structural changes in response to environmental perturbations, and for monitoring conformational changes due to ligand binding. It also provides a useful tool for probing molecular interactions, such as those associated with crystallization. Here we introduce the first commercial system specifically designed for high-throughput solution scattering experiments with macromolecules, the BioSAXS-1000. Comprised of specially designed focusing optics and a Kratky block, the BioSAXS-1000 system eliminates smearing issues common to traditional Kratky cameras. The system includes a high sensitivity pixel array detector and intuitive data collection software that includes full automation of the Kratky alignment hardware. Together, the many features of the BioSAXS-1000 system allow for synchrotron-quality SAXS data from a home laboratory source in as little as 15 to 30 minutes for most protein samples.