2017 May 17 - June 29
2017 October 11 - December 21
2017 Proposal deadline: 08/01/17
2017 BTR deadline: 09/10/17
The CHESS wiggler stations have certainly been among the
most, if not the most productive macromolecular beamlines in existence.
For more than a decade MacCHESS and CHESS have pioneered many aspects of
modern protein crystallography at storage rings and have helped catalyze
the present biostructure revolution. Structural biology at CHESS has
been tremendously successful and now utilizes three out of our four
highest intensity wiggler stations. These stations are oversubscribed by
about a factor of three.
To help satisfy the growing demand for crystallography facilities, the National Institute of General Medical Sciences (NIGMS) has provided funds to CHESS to upgrade the high intensity A1, F1 and F2 experimental stations. The goal of this multiyear upgrade program is to provide biological user with higher quality x-ray beams and facilities – first and foremost to deliver x-ray beam with higher intensity, better energy resolution, tunability and stability. During 1999 we are redesigning and replacing the x-ray optics room, housings, and monochromator optics on the F1 and F2 stations. A new collimating mirror will filter the high power white beam and reduce the enormous heat load on the x-ray monochromator crystals. Additional developments in x-ray beam diagnostics and position stabilization with feedback are planned. A faster computer network and more reliable software and computer equipment will enhance data collection.
Schematic drawing of the new F2 monochromator optimized for fast energy tunability and stability needed to improve Multiwavelength Anomalous Diffraction (MAD) data collection. The first crystal must be water-cooled to withstand large x-ray heat loads.
(Drawing: A. Pauling)