Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals

eLife

William I Weis¹  Oliver B Zeldin²  Axel T Brunger²  Monarin Uervirojnangkoorn²  Artem Y Lyubimov²  Johan Hattne³  Nicholas K Sauter⁴  Aaron S Brewster⁴ 

[1] Department of Neurology and Neurological Sciences, Howard Hughes Medical Institute, Stanford University, Stanford, United States;Department of Molecular and Cellular Physiology, Stanford University, Stanford, United States;Janelia Research Campus, Ashburn, United States;Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, United States;

关键词: X-ray crystallography;    free electron laser;    data processing;   

DOI  :  10.7554/eLife.05421

来源: DOAJ

【 摘 要 】

There is considerable potential for X-ray free electron lasers (XFELs) to enable determination of macromolecular crystal structures that are difficult to solve using current synchrotron sources. Prior XFEL studies often involved the collection of thousands to millions of diffraction images, in part due to limitations of data processing methods. We implemented a data processing system based on classical post-refinement techniques, adapted to specific properties of XFEL diffraction data. When applied to XFEL data from three different proteins collected using various sample delivery systems and XFEL beam parameters, our method improved the quality of the diffraction data as well as the resulting refined atomic models and electron density maps. Moreover, the number of observations for a reflection necessary to assemble an accurate data set could be reduced to a few observations. These developments will help expand the applicability of XFEL crystallography to challenging biological systems, including cases where sample is limited.

【 授权许可】

Unknown