Help Privacy Policy Disclaimer
  Advanced SearchBrowse




Book Chapter

Single particle imaging with FEL using photon correlations


von Ardenne,  B.
Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society;


Grubmüller,  H.
Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)

(Publisher version), 864KB

Supplementary Material (public)
There is no public supplementary material available

von Ardenne, B., & Grubmüller, H. (2020). Single particle imaging with FEL using photon correlations. In T. Salditt, A. Egner, & D. Luke (Eds.), Nanoscale Photonic Imaging (pp. 435-455). Cham: Springer. doi:10.1007/978-3-030-34413-9_16.

Cite as: https://hdl.handle.net/21.11116/0000-0007-1753-2
Scattering experiments with femtosecond high-intensity free-electron laser pulses provide a new route to macromolecular structure determination without the need for crystallization at low material usage. In these experiments, the X-ray pulses are scattered with high repetition on a stream of identical single biomolecules and the scattered photons are recorded on a pixelized detector. The main challenges are the unknown random orientation of the molecule in each shot and the extremely low signal to noise ratio due to the very low expected photon count per scattering image, typically well below the number of over 100 photons required by available analysis methods. The latter currently limits the scattering experiments to nano-crystals or larger virus particles, but the ultimate goal remains to retrieve the atomic structure of single biomolecules. Here, we use photon correlations to overcome the issue with low photon counts and present an approach that can determine the molecular structure de novo from as few as three coherently scattered photons per image. We further validate the method with a small protein (46 residues), show that near-atomic resolution of 3.3 Å is within experimental reach and demonstrate structure determination in the presence of isotropic noise from various sources, indicating that the number of disordered solvent molecules attached to the macromolecular surface should be kept at a minimum. Our correlation method allows to infer structure from images containing multiple particles, potentially opening the method to other types of experiments such as fluctuation X-ray scattering (FXS).