Beyond integration: modeling every pixel to obtain better structure factors from stills.

ABSTRACT: Most crystallographic data processing methods use pixel integration. In serial femtosecond crystallography (SFX), the intricate interaction between the reciprocal lattice point and the Ewald sphere is integrated out by averaging symmetrically equivalent observations recorded across a large number (10⁴-10⁶) of exposures. Although sufficient for generating biological insights, this approach converges slowly, and using it to accurately measure anomalous differences has proved difficult. This report presents a novel approach for increasing the accuracy of structure factors obtained from SFX data. A physical model describing all observed pixels is defined to a degree of complexity such that it can decouple the various contributions to the pixel intensities. Model dependenc

SUBMITTER: Mendez D 

PROVIDER: S-EPMC7642780 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature