Crystallization and Preliminary X-Ray Diffraction Studies of a 40 kDa Calcium Binding Protein Specifically Expressed in Plasmodia of Physarum polycephalum

抄録

A calcium binding protein with a molecular mass of 40 kDa (CBP40), the gene product of plasmodial-specific LAV1-2 of Physarum polycephalum, was crystallized in the presence of EDTA. The crystals diffracted X-rays up to a resolution of 3.0 A. They belonged to the trigonal space group, P3₂21 (or P3121), with unit cell dimensions of a=b=64.4 A and c=207.2 Å. Ca²⁺-bound crystals were obtained by soaking in a CaCl₂ solution, which gave diffraction data of similar quality. The Ca²⁺-soaked crystals belonged to the same space group as those crystallized in the presence of EDTA with unit cell dimensions of a=b=64.4 Å and c=209.4 Å.