Single crystal X-ray crystallography is a primary means of determining the molecular conformations of proteins and other biomolecules. It is thus critical for such applications as intelligent drug design and the characterization of medically-important effector targets.

The CLS boasts a highly-productive insertion device beamline (08ID-1) as well as a bending magnet beamline (08B1-1) with advanced capabilities that go beyond protein crystallography. Both beamlines are fully-equipped with on-axis visualization and the Stanford Automated Mounting System (SAM) allowing on-site or remote access. The facility has efficient software for sample and experiment tracking, data collection as well as an automated data processing pipeline. A humidity control device is available for controlled crystal dehydration experiments.


  • Single crystal X-ray crystallography for determining detailed structures of proteins and other molecules.
  • Determining protein structures with bound ligands for rational drug design.
  • Structural proteomics.
  • X-ray absorption spectroscopy (XAS), allowing high-resolution Extended X-ray Absorption Fine Structure (EXAFS) experiments on crystals to characterize metal centres.
  • Rapidly analyzing multi-component mixtures using powder diffraction methods to design pharmaceutical formulations and improve drug delivery systems.



Synchrotron advantages over conventional research techniques

  • Higher resolutions are usually attainable, allowing for more detailed structures
  • Spectral range of 4-18 keV allows for Single Anomalous Dispersion (SAD) and Multiple Anomalous Dispersion (MAD) experiments as well as characterization of a wide array of metal centres
  • High intensity of light allows for short experiment times on small sample sizes
  • Experimental phasing using sulfur is possible, which is naturally present in protein samples

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