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Collazo, M., Vaezeslami, S., Burl, S. (2014) Improving the crystallization process for optimal drug development. Am Lab March 28

mosquito crystal, 

mosquito LCP

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Macromolecular X-ray crystallography is an important and powerful technique in drug discovery. Studying the specific interactions of a particular drug with its protein target at the atomic level can help improve the drug design process.

Hundreds of different crystallization conditions need to be tested against a macromolecule of interest to grow crystals of sufficient size and quality and enable successful structure determination. With advanced synchrotron X-ray sources, crystals as small as 10 μm or less can now be used for X-ray diffraction, but typically various conditions are tested to obtain crystals of 50 μm or larger in size, to make the data collection easier and more robust.

The crystallization process can often prove inefficient, with only one or a few crystals produced from several hundred test conditions. Occasionally these crystals will be of sufficient quality for X-ray diffraction analysis and permit determination of the structure, which eliminates the need for further optimization of the conditions. However, in most cases the original “hits” may not form large enough crystals, only form precipitates, or generate poor or no diffraction at all. In these cases the crystallization conditions of the original hits need to be optimized. Obtaining these optimized and high-resolution diffracting crystals from targets of interest is vital to determining accurate molecular structures of these molecules.