Higher-throughput approaches to crystallization and crystal structure determination.
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.
Fogg
Mark J
MJ
Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York, UK.
Wilkinson
Anthony J
AJ
D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray / Q000379:methods*; D008967:Molecular Biology; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism
D011506:Proteins