Journal
JOURNAL OF APPLIED CRYSTALLOGRAPHY
Volume 38, Issue -, Pages 988-995Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S0021889805031572
Keywords
-
Categories
Ask authors/readers for more resources
High-throughput screening of a wide range of different conditions is typically required to obtain X-ray quality crystals of proteins for structure-function studies. The outcomes of individual experiments, i.e. the formation of gels, precipitates, microcrystals, or crystals, guide the search for and optimization of conditions resulting in X-ray diffraction quality crystals. Unfortunately, the protein will remain soluble in a large fraction of the experiments. In this paper, an evaporation-based crystallization platform is reported in which droplets containing protein and precipitant are gradually concentrated through evaporation of solvent until the solvent is completely evaporated. A phase transition is thus ensured for each individual crystallization compartment; hence the number of experiments and the amount of precious protein needed to identify suitable crystallization conditions is reduced. The evaporation-based method also allows for rapid screening of different rates of supersaturation, a parameter known to be important for optimization of crystal growth and quality. The successful implementation of this evaporation-based crystallization platform for identification and especially optimization of crystallization conditions is demonstrated using the model proteins of lysozyme and thaumatin.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available