Nature Methods
- 5, 147 - 153 (2008)
Published online: 30 January 2008; | doi:10.1038/nmeth.f.203
Protein crystallization: from purified protein to diffraction-quality crystalNaomi E Chayen1 & Emmanuel Saridakis21
Naomi E. Chayen is in the Department of Biomolecular Medicine, Division of Surgery, Oncology, Reproductive Biology and Anaesthetics, Faculty of Medicine, Imperial College London, Sir Alexander Fleming Building, London SW7 2AZ, UK. 2
Emmanuel Saridakis is at the Laboratory of Structural and Supramolecular Chemistry, Institute of Physical Chemistry, National Centre for Scientific Research "Demokritos", Ag. Paraskevi, 15310 Athens, Greece.
Correspondence should be addressed to Naomi E Chayen n.chayen@imperial.ac.uk Determining the structure of biological macromolecules by X-ray crystallography involves a series of steps: selection of the target molecule; cloning, expression, purification and crystallization; collection of diffraction data and determination of atomic positions. However, even when pure soluble protein is available, producing high-quality crystals remains a major bottleneck in structure determination. Here we present a guide for the non-expert to screen for appropriate crystallization conditions and optimize diffraction-quality crystal growth.
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