Overview

Protein Crystallography at the Alberta Synchrotron Institute

All of the Alberta Synchrotron Institute Protein Crystallography (PX) programs have one basic purpose, to support and aid researchers in Alberta working on protein structure determinations, particularly involving synchrotron radiation. The Alberta Synchrotron Institute is involved in four primary PX programs:

• development of the macromolecular crystallography facilities at the CLS
• arranging access to the Advanced Light Source Beamline 8.3.1
• outreach, training, and expertise development
• development of computational infrastructure for the ASI and associated synchrotron facilities

CLS Macromolecular Facilities

The Alberta Synchrotron Institute (ASI) is involved in the development of the macromolecular crystallography facilities at the CLS at the level of the beamline team (ASI PX Project Leader Dr. Ernst Bergmann and Prof. Bart Hazes, Medical Microbiology and Immunology, University of Alberta) and at the level of the board of directors of the CLS (Prof. Hans Vogel, Department of Biological Sciences, University of Calgary). These representatives contribute to the development of world class facilities for structural biology at the CLS and ensure the protection of the investments that Alberta's funding agencies have made in the CLS.

Additional macromolecular crystallography beamlines will be needed in the future at the CLS, because it is clear that the demands of the Canadian community of structural biologists will outpace the available capacity at the CLS for some time to come.

A proposal for a new CLS protein crystallography beamline, with an emphasis on developing software and hardware for high-throughput data collection, was also developed by the ASI, collaborators at UBC and elsewhere and the CLS. The capabilities of this beamline will be required for future developments in structural biology, including large-scale structural genomics and drug discovery projects.

Participating in ALS Beamline 8.3.1

The ASI and the University of California are collaborating in a Participating Research Team (PRT) on Beamline 8.3.1 at the Advanced Light Source (ALS). This provides Alberta with 24-48 hours of guaranteed access each month, the end result being that essentially all synchrotron-based crystallographic experiments of the structural biologists of Alberta are now conducted at the ALS. With the available time, virtually all protein crystals produced in Alberta are placed into the X-ray beam at BL8.3.1 within a month or less. This situation has increased the productivity and competitiveness of Alberta's crystallographers, and allows for rapid collection of data once diffraction-quality crystals are obtained. More detailed information about ASI access to BL8.3.1 is provided elsewhere on the ASI website.

Outreach and Training

The training, expertise development and outreach aspects of the PX project range from meetings, including the organisation of the Third Annual Western Canadian Structural Biology Workshop, to local workshop training sessions and also sending interested individuals to training sessions hosted at synchrotron sources in the US. Two workshops held early in 2003, Biological Applications of Small-angle X-ray Scattering and a Course on XtalView and one in 2004, Approaches to Membrane Protein Crystallisation, were very well received by the attendees and provided a wealth of international and local expertise.

Computational Infrastructure

The ASI PX group is responsible for many of the day to day networking and computational resources required by the ASI and also by remote data collection and synchrotron access. Coordinating data collection effectively at the ALS has required the creation of a web-based database of crystals that has greatly enhanced the productivity of beamline data collection teams, and we are now in the process of creating a remote access interface so that researchers in Alberta can interact with their experiments in California. This manner of data collection will be critical in the future, as remote data collection is expected to become standard operating procedure. This will significantly reduce costs and will greatly aid in streamlining the process of structure determination from protein crystals.