The development of high-throughput crystallography combined with the wealth
of already accumulated information about protein crystallization propertie
s requires constant revision of current crystallization screening procedure
s. Two complementary 6 x 4 matrix 'clear strategy screens' (CSS) have been
developed and tested on a number of previously non-crystallized proteins. T
he screens yielded diffraction-quality crystals of a wide range of proteins
(enzymes, transcription factors, structural proteins, etc.) in cases where
the applications of commercially available screens were unsuccessful. Both
their inherently simple design and their flexible nature provide an experi
menter with a logical platform for further modification and optimization. F
urthermore, the screens facilitate cryoprotection and potential incorporati
on of anomalous scatterers for multiple/ single-wavelength anomalous disper
sion (MAD/SAD) experiments.