The Pi-minimal Screen and the Pi-PEG Screen were developed at the MRC Laboratory of Molecular Biology (Cambridge, UK) for efficient crystallization screening of soluble proteins and integral membrane proteins, respectively [1]. Both screens are based on incomplete factorial design.
The unique formulation of both screens was generated following a strategy named Pi sampling[1] in order to create novel combinations of precipitants, buffers and additives across a standard 96-condition plate layout. Thus, the diversity amongst the crystallization conditions is ideal for initial screening.
Find more about the formulation, e.g. the employed buffer systems, of the Pi-minimal Screen at: www.jenabioscience.com/cms/en/1/catalog/1620/
Benefit from the experience of membrane protein crystallization at the MRC and read more about the Pi-PEG Screen under: www.jenabioscience.com/cms/en/1/catalog/1621/
Reference:
[1] Gorrec et al. (2011) Pi sampling: a methodical and flexible approach to initial macromolecular crystallization screening. Acta Cryst. D67:463.
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