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Protein Crystallization Strategies for Structural Genomics
Protein Crystallization Strategies for Structural Genomics

Editor: Naomi E. Chayen
Publisher: International University Line, 2007
ISBN-10: 097207743X ISBN-13: 978-0972077439
Hardcover: 290 pages
Getting from gene to structure involves many steps: cloning expression, solubilization, purification, crystallization, and only then, the determination of the structure. Once protein is pure and soluble, the key to crystallography is the availability of high quality
crystals. Producing high-quality crystals has always been the bottleneck to structure determination and with the advent of proteomics this problem is becoming increasingly acute. As a result, crystallization is gathering a new momentum as evidenced by the increasing numbers of commercial companies selling crystallization kits and tools, the increased investment of pharmaceutical companies in crystallization equipment and expertise, a high demand for practical courses in crystal growth, and the launch by the International Union of Crystallography of a new journal, Acta Crystallographica Section F, formed in 2005 for publishing the recent explosion of data concerning crystallization.

The past five years have seen some of the greatest achievements in the field of protein crystallization. It is now feasible to screen thousands of potential crystallization conditions by dispensing trials consisting of nanoliter volumes in a high-throughput mode. This has cut the time of setting up experiments from weeks to minutes, a scenario that was unimaginable a few years ago. Even more incredible, is the revelation that diffracting crystals can be produced from protein samples in volumes as small as 5–20 nanoliter. The subsequent phase of image capture and analysis of the crystallization drops is also progressing in great strides.

Surprisingly, in spite of the impressive advances accomplished, the crystallization problem has not been solved. High-throughput has not yet resulted in high output and the current challenge is to design new and improved techniques (of screening and optimization) for the production of useful crystals. Scientists worldwide have taken on the challenge by tackling the crystallization problem from a variety of different aspects.

Research advances in recent years have opened up the scope for the development of new methods and tools to overcome the bottleneck of protein crystallization. A variety of parameters that could previously not be explored are now accessible thanks to sophisticated apparatus and the development of new science-based techniques to monitor and control the process of crystallization. However, in order to become useful to the structural genomics effort, it is vital to miniaturize and automate these techniques and adapt them to cope with the vast numbers of “leads” resulting from the high-throughput screening procedures. Such efforts are those of the immediate future and the focus of this book. Naomi E. Chayen, Professor, Imperial College London.

1. Structural Genomics in the United States: The NIGMS Protein Structure Initiative
Charles G. Edmonds and John C. Norvell
2. A Guide To Automation and Data Handling in Protein Crystallization
3. Automated Liquid-Handling Systems for Submicroliter Crystallization
Terese Bergfors
4. Soft-Polymer Microfluidic Applications to Protein Crystallization
James M. Berger
5. Counter-Diffusion Capillary Crystallization for High-Throughput Applications
Juan M. Garcia-Ruiz and Joseph D. Ng
6. Scale-Down Approaches for Measuring Protein - Protein Interactions
Joseph C. Fanguy, Charles S. Henry, Steven C.Holman, Joseph J. Valente, and W. William
7. Gearing Optimization Techniques Towards High-Throughput
Naomi E. Chayen
8. Miniaturization and Automation for High-Throughput Membrane Protein Crystallization in
Lipidic Mesophases
Vadim Cherezov and Martin Caffrey
9. Automated Classification of Crystallization Experiments
Julie Wilson
HR5-230 Protein Cryst. Strategies for Structural Genomics each
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