ABSTRACT
The catalytic domain of death-associated protein kinase (DAPK) has been overexpressed, purified and crystallized using the sitting-drop vapour-diffusion method with PEG 8000 and magnesium acetate as precipitants. Complexes with the inhibitor staurosporine and its analogue BDB402 were also crystallized in the presence of PEG 400 and PEG 8000, respectively. Diffraction data were collected to 2.4 A for the native catalytic domain, to 2.9 A for the staurosporine complex and to 2.7 A for the BDB402 complex. All three crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 77.992, b = 109.909, c = 50.063 A for the catalytic domain, a = 78.911, b = 113.162, c = 50.658 A for the staurosporine complex and a = 77.337, b = 108.869, c = 50.186 A for the BDB402 complex. In both complexes the inhibitor molecule was clearly assigned in the difference Fourier map calculated on the basis of the phases obtained from the structure of the catalytic domain.
