Open AccessRadiation damage of protein crystals at cryogenic temperatures between 40 K and 150 K
Author(s) -
Teng TsuYi,
Moffat Keith
Publication year - 2002
Publication title -
journal of synchrotron radiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.172
H-Index - 99
ISSN - 1600-5775
DOI - 10.1107/s0909049502008579
Subject(s) - radiation damage , synchrotron radiation , monochromatic color , radiation , diffraction , irradiation , atmospheric temperature range , x ray , photon , range (aeronautics) , optics , synchrotron , materials science , physics , atomic physics , chemistry , nuclear physics , composite material , thermodynamics
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, 313317 ] 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.