Precipitation diagram and optimization of crystallization conditions at low ionic strength for deglycosylated dye-decolorizing peroxidase from a basidiomycete

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Shinya SaijoMakoto Shoda

Abstract

The growth of suitably sized protein crystals is essential for protein structure determination by X-ray crystallography. In general, crystals are grown using a trial-and-error method. However, these methods have been modified with the advent of microlitre dispensing-robot technology and of protocols that rapidly screen for crystal nucleation conditions. The use of one such automatic dispenser for mixing protein drops (1.3-2.0 microl in volume) of known concentration and pH with precipitating solutions (ejecting 2.0 microl droplets) containing salt is described here. The results of the experiments are relevant to a crystallization approach based on a two-step procedure: screening for the crystal nucleation step employing robotics followed by optimization of the crystallization conditions using incomplete factorial experimental design. Large crystals have successfully been obtained using quantities as small as 3.52 mg protein.

References

Apr 28, 1968·Journal of Molecular Biology·B W Matthews
Nov 1, 1995·Protein Science : a Publication of the Protein Society·C N PaceT Gray
Oct 1, 1996·Protein Engineering·N E Chayen
Nov 14, 1997·Structure·N E Chayen
Oct 8, 1998·Acta Crystallographica. Section D, Biological Crystallography·N E Chayen
Nov 28, 2002·Acta Crystallographica. Section D, Biological Crystallography·Gerlind SulzenbacherChristian Cambillau

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Citations

Nov 17, 2007·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Tomomi Ten-ITakao Sato
Nov 22, 2011·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·C Abad-ZapateroA Guasch

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