2.7.1.B20	crystallized as the apoenzyme as well as in complex with an ATP analogue and Mg2+. The latter crystal form is also soaked with D-fructose 6-phosphate. Synchrotron-radiation data are collected to 1.70 A for the apoenzyme crystals and 1.93 A for the complex crystals. All crystals exhibit orthorhombic symmetry. The apoenzyme crystals contain one monomer per asymmetric unit whereas the complex crystals contain a dimer	
2.7.1.B20	sitting nanodroplet vapor diffusion method, crystal structure of Ta0880, determined at 1.91 A resolution reveals a dimer with each monomer composed of an alpha/beta/alpha sandwich domain and a smaller lid domain	
2.7.1.B20	sitting- and hanging-drop vapour diffusion methods, three-dimensional structures of the unliganded enzyme and a complex of the enzyme, an ATP analogue and adenosine are determined to 1.7 and 1.9 A resolution, respectively. In the crystal structure of the MjNK complex, subunit A adopts a closed conformation and subunit B an open conformation. In subunit A all substrates and Mg2+ are observed, whereas in subunit B only the ATP analogue can be clearly identified in the electron density