Mission Statement

Biochemistry at the atomic scale 

Understanding essential biochemical processes at the atomic level is the key to discoveries in the bioenergy, biomedical, and pharmaceutical sciences. IMAGINE’s high resolution allows researchers to study proteins and other biomacromolecules, including those involved in processes such as biofuels production, the development of disease, and drug design..

Instrument Description

CG-4D’s IMAGINE instrument is a state-of-the-art, neutron image plate, 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 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).

Applications

Macromolecular structure and function

  • Hydrogen atoms in proteins
  • Enzymology
  • Ligand complexes
  • Structure-assisted drug design

Supra-Molecular Crystallography

  • Single molecule magnets (SMMs)
  • Metal-organic-frameworks (MOFs)
  • Polyoxometalates (POMs)

Sample Environment Under Development: Materials under Extreme Environment

  • 1 Mb and cryogenic temperatures
  • Phase transitions
  • Magnetic Transitions

 

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 Neutron image plate (Gd2O3 doped BaF(Br.I):Eu2+)
Detector size 1200 x 450 mm
Pixel size 125, 250, 500 µm
Sample-to-detector distance 200 mm
Goniometer Kappa and phi rotation axes

 

 

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