Using Dynamic Light Scattering to Improve Protein Solution Behavior for Crystallization

摘要

Improving protein solution behavior is critical in the field of structural biology since it impacts protein crystallization and the ability to determine protein structures by solution nuclear magnetic resonance (NMR) methods. Many proteins remain intractable to these powerful techniques because they are inherently unstable or have a tendency to form aggregates under typical buffer conditions. Dynamic light scattering (DLS) is a powerful tool capable of monitoring the aggregation state of protein molecules in solution, while also assisting in the initial generation and further optimization of protein crystals, through efficient and reliable optimization of protein solution behavior.1'2 More monodisperse protein samples often result in more crystallization hits in screening, and sometimes result in crystals with better diffracting properties compared to crystals arising from polydisperse protein samples.3 DLS is particularly effective if applied in conjunction with other methods used for characterizing protein behavior, including native poly-acrylamide gel electrophoresis (PAGE) and size-exclusion chromatography (SEC). The National Research Council-Biotechnology Research Institute (NRC-BRI) implements DLS and SEC to improve protein solution behavior for crystallization.