First Crystallography Results at the CLS
The afternoon of Saturday March 18 saw another important milestone for the CLS and the Canadian crystallography community, with the first x-ray diffractions taken on the Canadian Macromolecular Crystallography Facility (CMCF) beamline.
The images are of a protein crystal, PEP carboxykinase, provided by University of Saskatchewan professor and CMCF beam team leader Louis Delbaere.
Congratulations to the CMCF beamline team Pawel Grochulski and Alan Duffy, and CLS staffers Russ Berg, Henry Yee, Mike McKibben, Tony Wilson for all of their hard work to make this achievement possible, as well as CLS technologist Mark Besse, who brought the group luck that day!
Crystallography uses the diffraction patterns created when x-rays pass through a crystal to construct models of large molecules, such as proteins. Such knowledge allows scientists to understand how these complex substances interact chemically and how they can be manipulated at the molecular level, paving the way for new kinds of drugs.
While crystallography has been in use for decades using conventional x-ray sources, the brightness, tunability and coherent nature of synchrotron light allows the job to be done faster and with smaller crystals. Pharmaceutical companies all over the world now use synchrotrons as their tool of choice for their cutting-edge research.
For more information, visit:
CLS Experimental Facilities: http://www.lightsource.ca/experimental/cmcf.php
CMCF Beamline Website: http://ex.lightsource.ca/cmcf/
One of the first x-ray diffraction images taken on the CMCF beamline at the
CLS. l. (Exposure: 3s, Distance: 260 mm, E = 9.23 keV)
A view of the crystal from the beamline’s sample camera.
The crystal on the beamline. A stream of liquid nitrogen from a cryocooler (upper
right) keeps the crystal at -173 °C.
Last modified: 2012-01-19 17:01:54