Crystallization and preliminary crystallographic analysis of the NAD (H)-binding domain of Escherichia coli transhydrogenase.

Transhydrogenase is a proton-pumping membrane protein that is required for the cellular regeneration of NADPH. The NADPH- binding domain (domain I) of transhydrogenase from Escherichia coli was crystallized using the hanging-drop vapour-diffusion technique at room temperature. The crystals. which were grown from PFG 4000 and ammonium acetate in citrate buffer, belong to the triclinic space group P1, with unit-cell parameters a = 38.8, b = 68.8, c = 76.4 Å, α = 67.5, β = 80.8, γ = 81.5. X-ray diffraction data were collected to 1.9 Å resolution using synchrotron radiation. The crystals contain one dimer of transhydrogenase domain I per asymmetric unit. [ABSTRACT FROM AUTHOR]