Protein crystallization: from purified protein to diffraction-quality crystal.

Published on Feb 1, 2008in Nature Medicine30.64
· DOI :10.1038/nmeth.f.203
Naomi E. Chayen33
Estimated H-index: 33
(Imperial College London),
Emmanuel N. Saridakis52
Estimated H-index: 52
Abstract 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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