Sequential radiation damage in protein crystallography.
Radiation damage in protein crystals is described in terms of a sequential process of protein disordering. A new radiation-damage model has been tested against data from several protein crystals and can describe radiation damage corresponding to loss of the original intensity in excess of 80%. The model is an extension of previous models which characterize radiation damage in terms of successive conformational transitions of the protein from an undamaged to a spatially disordered to finally an amorphous state. The proposed model provides a more-general positional characterization of the disordered protein and includes, prior to the disordered state, a new dose-dependent state in which the protein conformation resembles the undamaged protein. Comparison of this model with the best previous model shows that the proposed model provides an improved fit to radiation-damage data.
Sygusch
J
J
Département de Biochimie, Faculté de Médecine, Université de Sherbrooke, Fleurimont, Québec, Canada.
Allaire
M
M
D000251:Adenosine Triphosphatases / Q000528:radiation effects; D000818:Animals; D003461:Crystallography; D005634:Fructose-Bisphosphate Aldolase / Q000528:radiation effects; D007700:Kinetics; D011487:Protein Conformation; D011506:Proteins / Q000528:radiation effects*; D011817:Rabbits
D011506:Proteins; D000251:Adenosine Triphosphatases; D005634:Fructose-Bisphosphate Aldolase