The BioSAXS-1000 and a new approach to combining visible and UV light imaging - the latest developments from Rigaku

Mark Benson

Rigaku Europe, Sevenoaks, Kent, UK

X-ray crystallography is a fundamental technique for obtaining atomic level structural information for macromolecules. However, the requirement for diffraction quality crystals often limits its efficacy for studying protein complexes or systems with inherent structural disorder. In such cases where crystallographic methods have failed, 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 conformation changes due to ligand binding.

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 photon counting hybrid 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.

Crystallization of proteins is a critical bottleneck in structural biology today. Prior to finding conditions that produce diffraction quality crystals, many hundreds of crystallization conditions must be examined.

The new Minstrel HT UV takes a novel approach to automated crystal imaging. Developed by Rigaku for high throughput imaging of crystallization plates, this instrument allows imaging of multiple plate types at a given temperature under a variety of imaging conditions, including black-and-white, color, polarized and UV.