CONFORMATIONAL CHANGE OF THE ADENOVIRUS DNA-BINDING PROTEIN-INDUCED BY SOAKING CRYSTALS WITH K3UO2F5 SOLUTIONS

Soaking crystals of the C-terminal DNA-binding domain of the adenoviru s single-stranded DNA-binding protein with a buffer containing K3UO2F5 results in a 9% change of the crystallographic c axis without destruc tion of the crystals or appreciable loss of resolution. The crystals b elong to space group P2(1)2(1)2(1) With a = 79.7, b = 75.6 and c = 60. 5 Angstrom. The three-dimensional structure has been refined to 2.7 An gstrom with a crystallographic R factor of 0.206. Antiparallel chains of protein molecules running through the entire crystal are linked by uranyl ions. The relative orientation of protein monomers is flexible, even in the crystalline state, and allows changes in the packing of t he protein chains.