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Joe Luft examines crystallization screening plates
Jennifer Wolfley using a liquid handling system to format plates
 
crystal
NEW!  Membrane protein crystallization screen

The high-throughput screening (HTS) laboratory, which is part of the Center for High-Throughput Structural Biology (CHTSB) at the Hauptman-Woodward Institute (HWI), will prepare crystal-growth screening experiments in 1536-well microassay plates for a nominal fee.  (This fee will be waived for users requesting the membrane protein crystallization screen.)  Experiments are started at approximately one-month intervals.  Although an effort is made to accommodate everyone as quickly as possible, there is a queue for sample submission, and a delay occasionally occurs.  In order to reserve a spot in the crystallization queue, you must return a completed high-throughput screening order form and wait for instructions telling you when your sample(s) can be submitted.  Click the appropriate button above to download the HTS Order Form for the standard screen.  For more information, contact the HTS Lab (htslab@hwi.buffalo.edu).

Information will not be publicly disclosed regarding any sample received for crystallization trials without the expressed written consent of the investigator(s).  However, investigators will be asked to give certain information about the target protein for inclusion in the crystallization database that is being compiled as part of the ongoing research program in crystal growth at HWI.  (Participation is voluntary, but is strongly encouraged and deeply appreciated.)  The database is composed largely of results from experiments conducted in the high-throughput laboratory, and it will be used to predict crystallization recipes for proteins that have never been crystallized successfully. The prediction algorithm depends on the identification of proteins that have been crystallized and are similar to the problem at hand.  Measures of similarity based on biochemical and biophysical properties are being devised.

If the high-throughput screening facility assists you in identifying initial crystallization conditions, then to help us track the use and success of the screening laboratory, we ask you to please reference one of the following articles:

Standard Screen. Luft, J. R., Collins, R. J., Fehrman, N. A., Lauricella, A. M., Veatch, C. K. & DeTitta, G. T. (2003). A deliberate approach to screening for initial crystallization conditions of biological macromolecules. J. Struct. Biol. 142, 170-179.  [PubMed ID: 12718929]

Membrane Screen.  Koszelak-Rosenblum, M., Krol, A., Mozumdar, N., Wunsch, K., Ferin, A., Cook, E., Veatch, C. K., Nagel, R., Luft, J. R., DeTitta, G. T & Malkowski, M. G. (2009). Determination and application of empirically derived detergent phase boundaries to effectively crystallize membrane proteins. Protein Science 18, 1828-1839. [Pub Med ID: 19554626]

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