Towards the spatial resolution of metalloprotein charge states by detailed modeling of XFEL crystallographic diffraction.

ABSTRACT: Oxidation states of individual metal atoms within a metalloprotein can be assigned by examining X-ray absorption edges, which shift to higher energy for progressively more positive valence numbers. Indeed, X-ray crystallography is well suited for such a measurement, owing to its ability to spatially resolve the scattering contributions of individual metal atoms that have distinct electronic environments contributing to protein function. However, as the magnitude of the shift is quite small, about +2 eV per valence state for iron, it has only been possible to measure the effect when performed with monochromated X-ray sources at synchrotron facilities with energy resolutions in the range 2-3 × 10^-4 (ΔE/E). This paper tests whether X-ray free-electron laser (XFEL) pulses, which hav

SUBMITTER: Sauter NK 

PROVIDER: S-EPMC7008510 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature