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Published online before print February 27, 2007
Protein Science, DOI: 10.1110/ps.062699707
 Copyright © 2007 The Protein Society
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Efficient optimization of crystallization conditions by manipulation of drop volume ratio and temperature

Joseph R. Luft1,2, Jennifer R. Wolfley1, Meriem I. Said1, Raymond M. Nagel1, Angela M. Lauricella1, Jennifer L. Smith1, Max H. Thayer1, Christina K. Veatch1, Edward H. Snell1,2, Michael G. Malkowski1,2, and George T. DeTitta1,2

1 Hauptman-Woodward Medical Research Institute, Buffalo, New York 14203, USA
2 Department of Structural Biology, SUNY at Buffalo, Buffalo, New York 14203, USA

(RECEIVED December 1, 2006; FINAL REVISION December 15, 2006; ACCEPTED December 20, 2006)

An efficient optimization method for the crystallization of biological macromolecules has been developed and tested. This builds on a successful high-throughput technique for the determination of initial crystallization conditions. The optimization method takes an initial condition identified through screening and then varies the concentration of the macromolecule, precipitant, and the growth temperature in a systematic manner. The amount of sample and number of steps is minimized and no biochemical reformulation is required. In the current application a robotic liquid handling system enables high-throughput use, but the technique can easily be adapted in a nonautomated setting. This method has been applied successfully for the rapid optimization of crystallization conditions in nine representative cases.

Keywords: protein crystallization; high throughput; optimization; temperature

Reprint requests to: Joseph R. Luft, Hauptman-Woodward Medical Research Institute, 700 Ellicott Street Buffalo, NY 14203, USA; e-mail: luft{at}hwi.buffalo.edu; fax: (716) 898-8660.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.062699707.


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Copyright © 2007 by The Protein Society.