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