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Reduction of X-ray-induced radiation damage of macromolecular crystals by data collection at 15 K: a systematic study

DOI: 10.1107/S0907444906053261 DOI Help
PMID: 17327667 PMID Help

Authors: A. Meents (Swiss Light Source) , A. Wagner (Diamond Light Source) , R. Schneider (Swiss Light Source) , C. Pradervand (Swiss Light Source) , E. Pohl (Swiss Light Source) , Clemens Schulze-Briese (Swiss Light Source)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section D Biological Crystallography , VOL 63 (3) , PAGES 302-–309

State: Published (Approved)
Published: March 2007

Abstract: The cryocooling of protein crystals to temperatures of around 100 K drastically reduces X-ray-induced radiation damage. The majority of macromolecular data collection is therefore performed at 100 K, yielding diffraction data of higher resolution and allowing structure determination from much smaller crystals. However, at third-generation synchrotron sources radiation damage at 100 K still limits the useful data obtainable from a crystal. For data collection at 15 K, realised by the use of an open-flow helium cryostat, a further reduction of radiation damage is expected. However, no systematic studies have been undertaken so far. In this present study, a total of 54 data sets have been collected from holoferritin and insulin crystals at 15 and 90 K in order to identify the effect of the lower data-collection temperature on the radiation damage. It is shown that data collection at 15 K has only a small positive effect for insulin crystals, whereas for holoferritin crystals radiation damage is reduced by 23% compared with data collection at 90 K.

Journal Keywords: cryocrystallography; radiation damage; helium cooling

Subject Areas: Biology and Bio-materials, Technique Development

Facility: X10SA at SLS

Added On: 16/04/2010 14:56

Discipline Tags:

Technique Development - Life Sciences & Biotech Structural biology Life Sciences & Biotech

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