Improved Efficiency at Protein Crystallography Beamlines through Automation

A. Cohen

Stanford Synchrotron Radiation Laboratory, SLAC, Stanford University, Stanford, CA 94309

Over the past five years the protein crystallography group at SSRL, has commissioned three new stations, increased computing capacity, added advanced control systems, and obtained fast readout CCD detectors, enabling experimenters to determine more structures in less time. Although throughput has increased by an order of magnitude, the demand for protein crystallography beam time at SSRL continues to exceed the supply. In particular as MAD and SAD techniques have become the methods of choice, the intense, rapidly tunable endstation BL9-2 has been over 200% oversubscribed since its coming online in 1999. To help address this demand, developments have been made in two areas: first the capabilities of the existing facility have been enhanced by automating energy changes on wiggler side-stations, and secondly the time required for screening samples has decreased by implementing robotic crystal mounting. Crystallographers at SSRL may now quickly screen a large number of crystals without delays from repeatedly entering the experimental hutch, and once a suitable crystal is found, they may rapidly optimize data collection parameters for a SAD or MAD experiment. The use, design and implementation of these systems will be described.

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