Article
Preparation and X-ray crystallographic analysis of rubredoxin crystals from Desulfovibrio gigas to beyond ultra-high 0.68 A resolution.
Biochemical and biophysical research communications - 5 Sept 2003
Chen Chun-Jung, Liu Ming-Yih, Chen Yi-Ting, LeGall Jean
Abstract excerpt
Rubredoxin (D.g. Rd), a small non-heme iron-sulfur protein shown to function as a redox coupling protein from the sulfate reducing bacteria Desulfovibrio gigas, has been crystallized using the hanging-drop vapor diffusion method and macroseeding method. Rubredoxin crystals diffract to an ultra-high resolution 0.68 A using synchrotron radiation X-ray, and belong to the space group P2(1) with unit-cell parameters...
Topics
- Crystallography, X-Ray
- Desulfovibrio
- Electrons
- Iron
- Models, Chemical
- Mutation
- Oxidation-Reduction
- Rubredoxins
- Sulfur
- X-Rays
