CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF RECOMBINANT HUMAN P38 MAP KINASE

The recombinant human p38 MAP kinase has been expressed and purified f rom both Escherichia coli and SF9 cells, and has been crystallized in two forms by the hanging drop vapor diffusion method using PEG as prec ipitant. Both crystal forms belong to space group P2(1)2(1)2(1). The c ell parameters for crystal form 1 are a = 65.2 Angstrom, b = 74.6 Angs trom and c = 78.1 Angstrom. Those for crystal form 2 are a = 58.3 Angs trom, b = 68.3 Angstrom and c = 87.9 Angstrom. Diffraction data to 2.0 Angstrom resolution have been collected on both forms.