The Bragg Crystallography Facility

Structure determination for small and large molecules

The Facility | Commercial Applications | Key People

Single-crystal X-ray structure determination provides the single most important means of unambiguously characterising
molecules in the solid state. Using this technique an experimenter can determine the exact 3-D arrangement of atoms in a structure - this includes the relative positions, bonding and interactions of all atoms in a structure. No single step can provide more information about the way a biological/chemical agent works than its three dimensional structure.

The Facility

The main capabilities of the Bragg Crystallography Facility include:

• High throughput small molecule structure determination
• Protein and macromolecule structure determination
• Screening of large protein samples for subsequent synchrotron data collection
• Powder diffraction analysis

Key equipment include two state-of- the-art diffractometers :

• a Mo-target Oxford Diffraction X-Calibur X-ray diffractometer for small molecule structure determination
• a Cu-target Rigaku Hiflux Homelab rotating anode X-ray diffractometer for large molecule structure determination.

Commercial Applications

1) High throughput small molecule structure determination (SMX)
SMX is used to determine the structures or inorganic, organic and mineralogical species (i.e. compounds with a few atoms to those containing a thousand atoms) and to define the absolute structure and configuration of chiral (asymmetric) compounds. SMX can be used to identify and characterise potential drug leads, protein inhibitors/activators and nanoscale/catalytic homogenous systems.

2) Protein and macromolecule structure determination (PX)
PX structure determination offers industries with a research focus in biotechnology, (stem) cell biology, biochemistry, biomedicine
and biotechnology single step access to the 3-D structure of a protein or enzyme. This information can be used to further understand drug targets or biological activity, for example. Our PX capable instrument can also be used for other macromolecular structure determination, e.g. polynucleic acids, polymers and supramolecular extended network materials. The services provided under items 1 and 2 can include:

• Selection and mounting of crystal specimens
• X-ray data collection
• Digital movies of crystals
• Face-indexed numerical absorption corrections (when needed)
• Structure solution and refinement
• Full crystallographic report with experimental details, figures, files, and tables of crystallographic data

3) Screening of weakly diffracting protein samples prior to synchrotron access
Samples that require more intense X-ray sources due to inherently weak X-ray diffraction using conventional sources can only be structurally determined using the intense X-ray beams provided by a synchrotron. Examples of these samples include membrane bound proteins and biomacromolecules with dimensions greater than 60 x 10-10m.
The Bragg Crystallography Facility will be able to screen samples locally, thereby allowing more sensitive species to be screened for the first time and providing a rapid screening facility for other weakly diffracting samples.

4) Powder
Powder samples can be run on the Xcalibur (Mo radiation only). However, only homogeneous powder samples with at most two chemical components are appropriate for the CCD diffractometer.

Key People

Dr Christopher Sumby
The Bragg Crystallography Facility School of Chemistry and Physics The University of Adelaide AUSTRALIA 5005
T: +61 8 8303 7406
F: +61 8 8303 4380
E: christopher.sumby@adelaide.edu.au