Cryo-protection of protein crystals in intense x-ray beams
- 1 January 1992
- journal article
- research article
- Published by AIP Publishing in Review of Scientific Instruments
- Vol. 63 (1) , 1177-1180
- https://doi.org/10.1063/1.1143127
Abstract
A focused white beam from existing synchrotrons has an intensity comparable with the monochromatic beams available from future undulator beamlines. The beam from station 9.5 on the SRS has therefore been used to examine the radiation damage caused within a protein crystal, cooled to near liquid nitrogen temperature. It was found that observable radiation damage occurred at doses comparable with those which have been observed in cryo‐electron microscopy. It would be possible to collect many data sets from the test lysozyme crystal before radiation damage occurred under these conditions. However, it would not be possible to collect a good quality data set from a single protein crystal of a few tens of microns in size, even at liquid nitrogen temperature.Keywords
This publication has 3 references indexed in Scilit:
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- Enhancement in resolution and lack of radiation damage in a rapidly frozen lysozyme crystal subjected to high-intensity synchrotron radiationJournal of Applied Crystallography, 1990
- Cryocrystallography of ribosomal particlesActa crystallographica Section B, Structural science, crystal engineering and materials, 1989