Laue Diffractometer

IMAGINE |  CG-4D | HFIR

Laue Diffractometer (IMAGINE)

Mission Statement

Biochemistry, biotechnology and drug design at the atomic scale 

Neutron macromolecular crystallography (NMX) provides unparalleled insight into the molecular mechanisms of biological macromolecules, resolving fundamental questions about enzyme catalysis and enabling new strategies for rational drug design. As the only experimental technique capable of directly determining the positions of hydrogen atoms in biomacromolecules, NMX reveals critical details of hydrogen bonding, protonation states, and proton transfer that underpin biochemical reactions and molecular recognition. With its high-resolution capabilities, IMAGINE-X will enable researchers to investigate proteins, nucleic acids, and their complexes at an unprecedented level of functional detail. These studies will elucidate enzyme mechanisms, guide the engineering of improved industrial enzymes, reveal the molecular basis of disease, and accelerate the development of next-generation therapeutics, vaccines, and other structure-based drug design strategies.

Instrument Description

CG-4D’s IMAGINE-X instrument is a state-of-the-art single-crystal diffractometer that provides atomic resolution information on inorganic, organic, metallo-organic, and macromolecular single crystals that enables their chemical, physical, and biological structure and function to be understood. IMAGINE-X benefits communities with interest in pharmaceuticals, minerals and materials, small molecules, molecular organo-metallic complexes and metal-organic frameworks and enables the neutron crystal structure of oligonucleotides and proteins to be determined at near atomic resolutions (1.5 Å).

The instrument has undergone significant upgrade with the design and installation of a new continuously operating dynamic nuclear polarization (DNP) system for nuclear polarization, a new suite of 74 silicon photo multiplier (SiPM) Anger camera detectors suite and new polarized optics and spin-flipper to control the spin state of each event. The new DNP system enables tunable control of hydrogen neutron scattering cross sections in situ within biological crystals during experiments, which will provide order of magnitude enhancements in data collection and in the visibility of hydrogen atoms in the resulting protein structures. The polarized incident beam option also provides enhanced sensitivity for probing weak magnetic scattering signals from magnetic materials.

Applications

Macromolecular structure and function

  • Hydrogen atoms in proteins
  • Enzyme mechanisms and enzyme engineering
  • Ligand complexes
  • Protein-protein and protein-nucleic acid complexes
  • Structure-assisted drug design

Supra-Molecular Crystallography

  • Single molecule magnets (SMMs)
  • Metal-organic-frameworks (MOFs)
  • Polyoxometalates (POMs) 
  • Phase transitions
  • Magnetic structures

Sample Environment: Materials under Extreme Environment

  • DNP - 5T magnetic field  and 1K  cryostat

 

Specifications

Flux ~107 n/s/cm2
Cross section 2.0 x 3.2 mm
Wavelengths minimum 2.0, 2.8, 3.3 Å
Wavelengths maximum 3.0, 4.0, 4.5 Å
Detector 74  silicon photo multiplier (SiPM) Anger cameras 
Detector size 2pi opening angle
Pixel size 500 µm
Sample-to-detector distance Variable – 350-600  mm
Goniometer Multi-axis Kappa, Phi, Omega cryo-goniometer operating at 1K

 

 

Drop Volume Calculator

 

 

The calculator assumes that only one crystal grows in the drop. Protein solubility is not considered. Accuracy of protein concentration is essential.
  a (Å) b (Å) c (Å) α (°) β (°) γ (°) Unit Cell Volume (Å3)
Custom Values
  Space group Number of asymmetric units Number of protein copies in asymmetric unit Target crystal volume (mm3) Protein concentration (mg/mL) Protein molecule weight (Da) Min volume to add (uL)
Custom Values
O’Dell W.B., Bodenheimer A., Meilleur F. (2016) Neutron protein crystallography: A complementary tool for locating hydrogens in proteins. Arch Biochem. Biophys. 602:48-60