Strategies for mitigating radiation damage and improving data completeness in 3D electron diffraction of protein crystals.

ABSTRACT: While 3D electron diffraction (3D-ED or microcrystal electron diffraction; MicroED) has emerged as a promising method for protein structure determination, its applicability is hindered by a high susceptibility to radiation damage, leading to a decreasing signal-to-noise ratio in consecutive diffraction patterns that limits the quality (resolution and redundancy) of the data. In addition, data completeness may be restricted due to the geometrical limitations of current sample holders and stages. Although specialized equipment can overcome these challenges, many laboratories do not have access to such instrumentation. In this work, we introduce an approach that addresses these issues using a commonly available 200 keV cryo-electron microscope. The multi-position acquisition technique that we

SUBMITTER: Shaikhqasem A 

PROVIDER: S-EPMC12809435 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature