Accurate macromolecular structures using minimal measurements from X-ray free-electron lasers

Nat Methods. 2014 May;11(5):545-8. doi: 10.1038/nmeth.2887. Epub 2014 Mar 16.

Abstract

X-ray free-electron laser (XFEL) sources enable the use of crystallography to solve three-dimensional macromolecular structures under native conditions and without radiation damage. Results to date, however, have been limited by the challenge of deriving accurate Bragg intensities from a heterogeneous population of microcrystals, while at the same time modeling the X-ray spectrum and detector geometry. Here we present a computational approach designed to extract meaningful high-resolution signals from fewer diffraction measurements.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacillus / enzymology
  • Calcium / chemistry
  • Calibration
  • Computer Simulation
  • Crystallization
  • Crystallography, X-Ray
  • Electrons
  • Equipment Design
  • Lasers*
  • Likelihood Functions
  • Macromolecular Substances / chemistry*
  • Models, Chemical
  • Molecular Conformation
  • Muramidase / chemistry
  • Nanotechnology
  • Reproducibility of Results
  • Software
  • Thermolysin / chemistry
  • X-Rays
  • Zinc / chemistry

Substances

  • Macromolecular Substances
  • Muramidase
  • Thermolysin
  • Zinc
  • Calcium

Associated data

  • PDB/4OW3