Protein Modification for Crystallization

Abstract

Technological advances in data collection with synchrotron radiation sources and phasing methods includ- ing automated model building and validation have highlighted crystallization as the rate-limiting step in X- ray diffraction studies of macromolecular structures. Although protein crystallization remains a stochastic event, protein engineering with the advent ofrecombinant methods enables us to generate target proteins possessing a higher propensity to form crystals suitable for X-ray diffraction data collection. This chapter presents an overview of protein engineering methods designed to enhance crystallizability and discusses examples of their successful application.