Crystallization and preliminary X-ray crystallographic studies of rusticyanin from Thiobacillus ferrooxidans.
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.
Djebli
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Case Western Reserve University, School of Medicine, Department of Biochemistry, Cleveland, OH 44106-4935.
Proctor
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Blake
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Shoham
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D001400:Azurin / Q000031:analogs & derivatives* / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D013855:Thiobacillus / Q000737:chemistry*; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; C012543:rusticyanin; D001400:Azurin