The many faces of radiation-induced changes.
During diffraction experiments even cryo-cooled protein crystals can be significantly damaged due to chemical and physical changes induced by absorbed X-ray photons. The character and scale of the observed effects depend strongly on the temperature and the composition of crystals. The absorption of radiation energy results in incremental regular changes to the crystal structure, making its impact on the process of solving the structure strongly correlated with other experimental variables. An understanding of all the dependencies is still limited and does not allow for a precise prediction of the outcome of a particular diffraction experiment. Results are presented of diffraction experiments performed under different experimental conditions. The influence of temperature and crystal composition on different characteristics of radiation damage is analyzed. The observed effects are discussed in terms of their impact on data processing and phasing procedures.
Borek
Dominika
D
Department of Biochemistry, University of Texas, Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA.
Ginell
Stephan L
SL
Cymborowski
Marcin
M
Minor
Wladek
W
Otwinowski
Zbyszek
Z
D003198:Computer Simulation; D018360:Crystallography, X-Ray / Q000379:methods*; D004307:Dose-Response Relationship, Radiation; D008956:Models, Chemical; D008958:Models, Molecular; D011487:Protein Conformation / Q000528:radiation effects; D011489:Protein Denaturation / Q000528:radiation effects; D011506:Proteins / Q000737:chemistry* / Q000528:radiation effects* / Q000648:ultrastructure; D011829:Radiation Dosage; D014965:X-Rays
D011506:Proteins