Record protein imaging resolution could be bridge to quantum crystallography

A 3d chemical protein structure with a heat map laid over.

Source: © Ashwin Chari/Max Planck Institute for Multidisciplinary Sciences & Gleb Bourenkov/European Molecu

Exceptional resolution a move towards mapping distribution of electrons in proteins

A new record has been achieved in protein imaging, capturing the protein rubredoxin at an unprecedented resolution of 0.43 angstroms, revealing structural features at a level rarely achieved for biological macromolecules.1

The measurement was made using x-rays from Petra III in Hamburg, Germany, the world’s brightest synchrotron source. Previous experiments, in which the team explored how x-rays interact with and alter protein structures, as well as how radiation damage can affect collected data, allowed them to develop a protocol that minimises damage while collecting diffraction data from protein crystals.2