Small-angle X-ray scattering (SAXS) is an important technique for generating low resolution structures of proteins in native solution. Moreover, SAXS provides information on aggregation, folding, unfolding, assembly and conformational changes of proteins in solution despite of the low resolution. BioSAXS-1000 is a two dimensional compact Kratky camera for SAXS measurements of biological macromolecules. BioSAXS-1000 can be installed on a new Rigaku microfocus X-ray generator, such as the MicroMax-007 HF, FR-E+SuperBright or MicroMax-003, or on an existing Rigaku microfocus X-ray generator with an open port.
For the purpose of protein structure determination, one often uses X-ray crystallography, electron crystallography and NMR spectroscopy. X-ray and electron crystallography are methods for determining three dimensional structures of high molecular weight protein complexes at atomic resolution. However, X-ray and electron crystallography require single crystals or two-dimensional crystals, respectively. Furthermore, the crystal structures from X-ray and electron crystallography are static, restrained by the packing energy of the crystal. NMR spectroscopy requires stable isotope labeling and multi-dimensional experiments. Moreover, NMR spectroscopy has molecular weight limitations.
Proteins are highly dynamic, and conformational and ordered-disordered structural changes play a crucial role in their functions. Static structural information is not suf?cient for investigating protein function. SAXS determines the dynamic three-dimensional solution structures of proteins in various solution conditions. The acquired diverse information is useful both pre- and post-structure determination by X-ray crystallography. SAXS provides complementary structure information for structural biology.
BioSAXS-1000 is a powerful tool to investigate dynamic structural biology.