In recent times, there has been a large increase in the number of protein structures deposited in the Protein Data Bank. Structural genomics initiatives have contributed to this expansion through their focus on high-throughput structural determination. This has fuelled advances in many of the techniques in the pipeline from gene to protein to crystal to structure. These include ligation-independent cloning methods, parallel purification systems, robotic crystallization devices and automated methods of crystal identification, data collection and, in some cases, structure solution. Some of these advances are described and discussed briefly with an emphasis on activities in the York Structural Biology Laboratory through its participation in the Structural Proteomics in Europe consortium.
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August 2008
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Conference Article|
July 22 2008
Higher-throughput approaches to crystallization and crystal structure determination
Mark J. Fogg;
Mark J. Fogg
1Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5YW, U.K.
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Anthony J. Wilkinson
Anthony J. Wilkinson
1
1Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5YW, U.K.
1To whom correspondence should be addressed (email ajw@ysbl.york.ac.uk).
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Biochem Soc Trans (2008) 36 (4): 771–775.
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Received:
April 07 2008
Citation
Mark J. Fogg, Anthony J. Wilkinson; Higher-throughput approaches to crystallization and crystal structure determination. Biochem Soc Trans 1 August 2008; 36 (4): 771–775. doi: https://doi.org/10.1042/BST0360771
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