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- ACS Fall
Aug 22-26, Boston, Massachusetts, USA - 3rd EuCheMS Chemistry Congress
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Cryo-Crystallography Options
Cryo-crystallography at crystal temperatures around 100 Kelvin has become the state-of-the-art in structural biology. The technique offers a number of advantages so obvious that room temperature measurements are not even considered. The most prominent benefits are:
- Smaller number of crystals for a complete data collection required since radiation damage due to radical diffusion is stopped or slowed down
- Increased diffraction intensities and higher diffraction resolution limit since thermal motion is decreased
- Crystals can be screened in-house, stored at cryogenic temperatures prior to the synchrotron trip
- The use of Cryo-Loops significantly lowers background diffraction compared to capillaries providing better signal to noise ratios
Commonly, crystals are ‘flash-cooled’, which means a crystal is placed quickly in a 100 K gas stream. However, not all protein crystals undergo the quick temperature drop without a loss in crystallinity. Individual cryo-conditions may need to be established. In general this involves empirical tests of cryo-protection agents. Usually, the tests are carried out on an in-house system prior to a planned synchrotron trip. Reliable and well established solutions are fully integrated into our Structural Biology solutions:

