Abstract
Cryocrystallography of biological macromolecules is an underused technique for improving the quality of crystallographically determined structures. Although the technique may not be useful in all cases, a growing number of examples show that radiation damage, protein instability or thermal motion can be greatly reduced by collecting X-ray diffraction data at cryogenic temperatures. Most macromolecular crystals can be cooled rapidly and diffract at least as well as they do at room temperature, although showing increased mosaic character.
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