Radiation damage of protein crystals at cryogenic temperatures between 40 K and 150 K.
X-ray radiation damage of lysozyme single crystals by an intense monochromatic beam from the Advanced Photon Source is studied at cryogenic temperatures between 40 K and 150 K. The results confirm that primary radiation damage is both linearly dependent on the X-ray dose and independent of temperature. The upper limit for the primary radiation damage observed in our previous study [Teng & Moffat (2000), J. Synchrotron Rad. 7, 313-317] holds over the wider temperature range of this study. The X-ray diffraction quality of the data acquired at 40 K is superior to those at 100 K, apparently due to temperature dependence of secondary and tertiary radiation damage and to reduced thermal motion.
Teng
Tsu-Yi
TY
Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA. t-teng@uchicago.edu
Moffat
Keith
K
D000818:Animals; D002645:Chickens; D003080:Cold Temperature; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D006801:Humans; D009113:Muramidase / Q000737:chemistry / Q000528:radiation effects*; D011506:Proteins / Q000528:radiation effects; D017356:Synchrotrons; D013696:Temperature
D011506:Proteins; C421864:hen egg lysozyme; D009113:Muramidase