Abstract
Technological advances in data collection with synchrotron radiation sources and phasing methods including 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 of recombinant 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.
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Hakoshima, T. (2016). Protein Modification for Crystallization. In: Senda, T., Maenaka, K. (eds) Advanced Methods in Structural Biology. Springer Protocols Handbooks. Springer, Tokyo. https://doi.org/10.1007/978-4-431-56030-2_9
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DOI: https://doi.org/10.1007/978-4-431-56030-2_9
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