Author:
Santarsiero B. D.,Yegian D. T.,Lee C. C.,Spraggon G.,Gu J.,Scheibe D.,Uber D. C.,Cornell E. W.,Nordmeyer R. A.,Kolbe W. F.,Jin J.,Jones A. L.,Jaklevic J. M.,Schultz P. G.,Stevens R. C.
Abstract
An approach that enables up to a two order of magnitude reduction in the amount of protein required and a tenfold reduction in the amount of time required for vapor-diffusion protein crystallization is reported. A prototype high-throughput automated system was used for the production of diffraction-quality crystals for a variety of proteins from a screen of 480 conditions using drop volumes as small as 20 nL. This approach results in a significant reduction in the time and cost of protein structure determination, and allows for larger and more efficient screens of crystallization parameter space. The ability to produce diffraction-quality crystals rapidly with minimal quantities of protein enables high-throughput efforts in structural genomics and structure-based drug discovery.
Publisher
International Union of Crystallography (IUCr)
Subject
General Biochemistry, Genetics and Molecular Biology
Cited by
223 articles.
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