Is radiation damage dependent on the dose rate used during macromolecular crystallography data collection?
This paper focuses on the radiation-damage effects when applying the same total X-ray dose to protein crystals at different dose rates. These experiments have been performed on both a selenomethionated protein and on bovine trypsin using dose rates that span nearly two orders of magnitude. The results show no clear dose-rate effect on the global indicators of radiation damage, but a small measurable dose-rate effect could be found when studying specific radiation damage. It is hypothesized that this observed dose-rate effect relates to differences in the steady-state free-radical concentration.
Leiros
Hanna Kirsti S
HK
Macromolecular Crystallography Group, European Synchrotron Radiation Facility (ESRF), 6 Rue Jules Horowitz, 38043 Grenoble, France.
Timmins
Joanna
J
Ravelli
Raimond B G
RB
McSweeney
Seán M
SM
D000818:Animals; D002417:Cattle; D018360:Crystallography, X-Ray; D003545:Cysteine / Q000737:chemistry / Q000378:metabolism; D003625:Data Collection; D034301:Deinococcus / Q000201:enzymology*; D004307:Dose-Response Relationship, Radiation; D005959:Glucosidases / Q000737:chemistry* / Q000528:radiation effects*; D008958:Models, Molecular; D011487:Protein Conformation; D011489:Protein Denaturation / Q000528:radiation effects; D012645:Selenomethionine / Q000737:chemistry / Q000378:metabolism; D017356:Synchrotrons; D014357:Trypsin / Q000737:chemistry* / Q000528:radiation effects*; D014965:X-Rays / Q000009:adverse effects*
D012645:Selenomethionine; D005959:Glucosidases; C099156:maltooligosyl trehalose trehalohydrolase; D014357:Trypsin; D003545:Cysteine