Journal
NATURE METHODS
Volume 5, Issue 2, Pages 147-153Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NMETH.F.203
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Funding
- EPSRC [EP/D501113/1] Funding Source: UKRI
- Engineering and Physical Sciences Research Council [EP/D501113/1] Funding Source: researchfish
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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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