Crystallization of F1F0-ATP synthase from Chloroflexus aurantiacus

Abstract Crystallization of F 1 F 0 -ATP synthase from thermophilic bacterium Chloroflexus aurantiacus was carried out in the present work. A new crystallization method based on slow detergent removal in a two-phase system, consisting of decane and protein solution, was developed. Three-dimensional protein crystals were grown by this method. Two-dimensional molecular lattice with unit cell parameters of a =28 nm, b =23 nm and φ =104° was observed by atomic force microscopy on their surface. Thickness of protein surface layer of the crystals was determined also. Model of the protein molecular packing of the crystals is suggested basing on the experimental data.