The Biochemistry Department houses all the equipment necessary for analyzing macromolecular crystals by low-powered X-ray diffraction.
Using X-ray crystallography, we can determine three-dimensional structure of a molecule. This method involves the purification of a protein, arranging the molecules in a regular lattice by crystallization, and exposing the crystals to an x-ray beam. The regularly spaced atoms within the array will generate a unique diffraction pattern, which can be used to solve the structure of the molecule of interest. These macromolecules can be proteins, nucleic acids or any other large complex.
In the Biochemistry Department we have the means to purify and crystallize proteins, nucleic acids and other biomolecular complexes and determine their 3D structure:
We have a Scorpion liquid handler robot (provided by Jeffrey Lee, LMP) to create and optimized crystallization screens.
We have a Gryphon Nanodrop robot that can be used to set up arrays of 50 nanoliter droplets to minimize the amount of protein or complex needed to perform crystalogenesis screens. This robot also has special features allowing for the crystallization of membrane proteins in Lipid cubic phase or bicelles.
We have a RockImager 1000 that is an automated crystal imager that can collect UV and visible light images to help identify protein crystals. We also have stereo dissecting microscopes to help loop the crystals and mount them in an x-ray beam to examine diffraction quality.
Diffracting crystals are exposed to X-rays generated by a Rigaku 007 rotating copper anode with two sets of optics and two Mar research detectors.
Medical Sciences Building
Room 5354 (x-ray room)
Room 5357 (crystalogenesis equipment)
University of Toronto
Coordinators and Contacts
Rm 5366 Medical Sciences Building
1 King's College Circle