Overexpression, crystallization, and preliminary X-ray crystallographic analysis of a putative Diguanylate cyclase from Thermotoga maritima by the Tm0107 gene

Bis-(3 ,5 )-cyclic-dimeric-guanosine monophosphate (c-di-GMP), a bacterial secondary messenger, is a crucial regulator of collective versus individual behavior in bacteria. Diguanylate cyclases (DGCs) are essential for the synthesis of c-di-GMP. To elucidate the structural features of DGCs, we initiated the crystallization of a putative DGC (Tm0107) from Thermotoga maritima. Tm0107 protein was overexpressed in Escherichia coli and crystallized at 295 K using PEG 3000 as a precipitant. Crystals of Tm0107 protein diffracted to 2.1 Å resolution and belong to a Tetragonal space group P4 3 2 1 2, with unit cell parameters of a = 61.3 Å, b = 61.3 Å and c = 101.1 Å. The crystallization of selenomethionine-substituted protein is in progress to solve the crystal structure of Tm0107 protein.