期刊
JOURNAL OF SYNCHROTRON RADIATION
卷 9, 期 -, 页码 198-201出版社
BLACKWELL MUNKSGAARD
DOI: 10.1107/S0909049502008579
关键词
protein crystals; radiation damage; monochromatic radiation
资金
- NCRR NIH HHS [RR07707] Funding Source: Medline
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.
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