- ASU Hosts Nozzle Maker Workshop
- XFEL Science Highlighted in Nature
- BioXFEL researchers capture the highest-resolution protein snapshots ever taken with an X-ray laser, revealing new details in a well-studied protein that acts as an “eye” in bacteria.
- BioXFEL Graduate Student Joey Olmos (Rice) Earns NSF Graduate Research Fellowship
- Science Director Dr. John Spence named Royal Society Fellow
- Tuesday, 16 February 2016 12:57
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.