Resolution and dose dependence of radiation damage in biomolecular systems.

ABSTRACT: The local Fourier-space relation between diffracted intensity I, diffraction wavevector q and dose D, , is key to probing and understanding radiation damage by X-rays and energetic particles in both diffraction and imaging experiments. The models used in protein crystallography for the last 50 years provide good fits to experimental I(q) versus nominal dose data, but have unclear physical significance. More recently, a fit to diffraction and imaging experiments suggested that the maximum tolerable dose varies as q ^-1 or linearly with resolution. Here, it is shown that crystallographic data have been strongly perturbed by the effects of spatially nonuniform crystal irradiation and diffraction during data collection. Reanalysis shows that

SUBMITTER: Atakisi H 

PROVIDER: S-EPMC6830208 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature