Increasing the success in obtaining structures and maximizing the value of the structures determined are the two major goals of target selection in structural proteomics. This chapter presents an efficient and flexible target selection procedure supplemented with a Web-based resource that is suitable for small- to large-scale structural genomics projects that use crystallography as the major means of structure determination. Based on three criteria, biological significance, structural novelty, and “crystallizability,” the approach first removes (filters) targets that do not meet minimal criteria and then ranks the remaining targets based on their “crystallizability” estimates. This novel procedure was designed to maximize selection efficiency, and its prevailing criteria categories make it suitable for a broad range of structural proteomics projects.
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Acknowledgments
The authors thank Tim Ravasi, Munish Puri, Ian Ross, Tom Alber, and all the members of the macrophage protein group for their feedback and advice. This work was supported by an Australian Research Council (ARC) grant to JLM and BK. BK is an ARC Federation Fellow and a National Health and Medical Research Council Honorary Research Fellow, and NC an Australian Synchrotron Research Program Fellow.
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Robin, G. et al. (2008). A General Target Selection Method for Crystallographic Proteomics. In: Kobe, B., Guss, M., Huber, T. (eds) Structural Proteomics. Methods in Molecular Biology™, vol 426. Humana Press. https://doi.org/10.1007/978-1-60327-058-8_2
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