- NSF awards $22.5 million to capture biology at the atomic level using X-ray lasers
- Frankuchen Award : ACA 2019
- BioXFEL Research Support Call for Proposals
- Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature
- UWM researchers create first 3D movie of virus in action
- Tuesday, 16 February 2016
Protein structure determination by X-ray crystallography is often limited by lack of access to high-quality crystals that generate sufficiently detailed diffraction patterns. However, X-ray patterns usually also contain continuous diffraction, which is largely ignored but could in principle provide sufficient information to overcome this limitation.
Kartik Ayyer and colleagues now show that the continuous diffraction arising from lattice disorder indeed enables structure determination. They use data collected from imperfect crystals of the protein complex photosystem II to obtain an image at 3.5 Å resolution. The method puts great value in commonly encountered imperfect crystals, and is expected to enable direct high-resolution structure determination for a range of macromolecular systems.