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Xylulose 5-phosphate (X5P) phosphoketolase (PK) is a central enzyme of the pentose phosphate pathway and in the same time, the largest representative of the thiamin diphosphate-dependent enzymes. In the presence of inorganic phosphate this enzyme converts X5P into glyceraldehyde 3-phosphate and acetyl phosphate. The ptk gene of PK from Lactococcus lactis was amplified by PCR and introduced into a prokaryotic expression vector. The enzyme was expressed as a fusion protein and purified by affinity and gel filtration chromatography. The purified protein thus obtained was electrophoretically homogeneous. The crystallization trials were performed using both hanging drop and sitting drop vapor diffusion techniques. Hanging drop procedure proved to be more efficient than sitting drop alternative procedure. Initially, crystal clusters were obtained; further optimization of protein purification as well as of crystallization conditions led to single crystals. X-ray diffractional tests on the crystals thus obtained evidenced that the crystals diffracted to approximately 3 Å. However the quality of the diffractional data still needs further improvement.

Polymer and co-polymer surface modifying effects in the protein crystallization