title: Crystallization and preliminary X-ray crystallographic studies of rusticyanin from Thiobacillus ferrooxidans.
abstract: Rusticyanin is a 16.5 kDa type I blue copper protein isolated from Thiobacillus ferrooxidans. This organism can grow on Fe2+ as its sole energy source. Rusticyanin is thought to be a principal component in the iron respiratory electron transport chain of T. ferrooxidans. As a component of the periplasmic space of an acidophilic bacterium, rusticyanin is remarkably stable at acidic pH. It is redox-active down to pH 0.2. Crystals of rusticyanin have been grown from solutions of PEG 8000 by the hanging-drop vapor diffusion method. The crystals are orthorhombic, space group P2(1)2(1)2(1), with unit cell dimensions a = 32.36 A, b = 60.37 A, c = 74.60 A. The crystals diffract to 2.0 A resolution and they are stable in the X-ray beam for at least two days.
authors.affiliation: Case Western Reserve University, School of Medicine, Department of Biochemistry, Cleveland, OH 44106-4935.
authors.forename: A
authors.initials: A
authors.lastname: Djebli
authors.forename: P
authors.initials: P
authors.lastname: Proctor
authors.forename: R C
authors.initials: RC
authors.lastname: Blake
authors.forename: M
authors.initials: M
authors.lastname: Shoham
mesh_terms: D001400:Azurin / Q000031:analogs & derivatives* / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D013855:Thiobacillus / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; C012543:rusticyanin; D001400:Azurin