Core Facilities of the London Regional Proteomics Centre
- Biomolecular Interactions and Conformations Facility
- Functional Proteomics Facility
- Biomolecular NMR Facility
- Biological Mass Spectrometry Laboratory
- MALDI Mass Spectrometry Facility
Links to other Schulich Core Facilities
New User?
Not a problem. Please take the time to review our:
Welcome to the Macromolecular Crystallography Facility
Within The Facility
The MCF houses a rotating anode generator and advanced optical system that supplies an intense, monochromatic, and well-collimated X-ray beam. The detector is a high resolution image plate system that is able to record diffraction from crystals with unit cell edges up to 300 Å.
We have the items necessary for both initial screenings and optimizations of crystal growth, including:
How We Can Help You
The MCF provides a full crystallization service, one where clients may send us samples or themselves gain access to sophisticated equipment and technologies, as well as receive advice and technical assistance in sample preparation and experimentation. You, the user, will be provided with screen preparation, plate setup, image acquisition and (if desired) optimization design.
In summary, we offer:
Analysis
After diffracting crystals are obtained, computers and software are available for the computation-intensive steps of data processing, reduction, and analysis, as well as graphics-intensive model-building and refinement.
Also from this web page:
About
The Macromolecular Crystallography Facility (MCF) is an analytical service laboratory which aims to screen for conditions that will crystallize protein samples, and then use X-ray diffraction to determine the three-dimensional, single-crystal structures of these macromolecules.
The MCF is part of the Biochemistry Department at the University of Western Ontario.
We are one of the 6 constituent core facilities of the London Regional Proteomics Centre, and are conveniently located in Room 333 of the Medical Sciences building.
Background
X-ray Crystallography is a method used for solving 3D structures of macromolecules at atomic resolution. This technique is widely used to study the structures of proteins, DNA, as well as complexes of proteins with inhibitors, substrates, nucleic acids and drugs.
The 3D structure of a protein can be used to understand biological processes at the most basic level; it is an essential component in understanding how and which molecules within a protein interact, as well as the mechanism with which a protein uses to carry out its function or interacts with other molecules.
