Introduction

Protein expression in E. coli is an efficient and commonly used method to generate large quantities of protein forresearch or therapeutic applications. Unfortunately, proteins expressed at high levels in E. coli are oftenpackaged into inclusion bodies (IBs). These tightly packed structures have the advantage of being composed ofalmost pure expressed protein, but the serious disadvantage that the protein is so tightly aggregated that highconcentrations of chaotropes or detergents are required to extract soluble protein from the aggregates. Thesesolubilization reagents must then be diluted or removed by buffer exchange, so that the extracted protein can berefolded into its native, functional conformation.