Application

Efficient crystallization screening of soluble proteins

Format

Bulk – 96 screening solutions in 10 ml aliquots
HTS – 96 screening solutions delivered in a deep-well block, 1.7 ml per well

The Pi-minimal Screen was developed at the MRC Laboratory of Molecular Biology (Cambridge, UK) for efficient crystallization screening of soluble proteins [1]. The approach is based on incomplete factorial design.

The unique formulation 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.

The Pi-minimal Screen includes 36 components, i.e. 12 precipitants, 12 buffers systems and 12 salts.
Buffers employed in the Pi-minimal screen are buffer systems (acid-base pairs, e.g. HEPES and HEPES sodium salt). Consequently, pH can be adjusted by mixing 2 stock solutions at different ratios during later optimizations.

The efficiency of the Pi-minimal Screen was demonstrated by the crystallization of 10 proteins before its commercialization [1].

Please make sure you also check out the Pi-PEG Screen!

   Flyer Pi-Screens (PDF, 1.1 MB)

Individual Conditions of all screens are available in 10 ml as well as 100 ml volumes. Please follow this link.

   Description how the JBScreen buffers are prepared

[1] Gorrec et al. (2011) Pi sampling: a methodical and flexible approach to initial macromolecular crystallization screening. Acta Cryst. D67:463.

Available online at http://journals.iucr.org/d/issues/2011/05/00/bw5391/index.html

   Download PDF (356 kB)

Please contact xtals@jenabioscience.com with questions or inquiries.