Crystal Structure of SCO6571 from Streptomyces coelicolor A3(2)
Abstract:SCO6571 protein from Streptomyces coelicolor A3(2) was overexpressed and purified using Rhodococcus erythropolis as an expressing host. Crystals of selenomethionine-substituted SCO6571 have been obtained by vapor diffusion method. SCO6571 crystals diffract to 2.3 Å and were found to belong to the orthorhombic space group P212121 with unit cell parameters a = 84.5, b = 171.6, c = 184.8 Å. Six molecules in the asymmetric unit give a crystal volume per protein mass (VM) of 2.97 Å3 Da-1 and solvent content of 58.6 %. The structure was solved by the single wavelength anomalous diffraction (SAD) method. SCO6571 is a TIM-barrel fold protein that assembles into a hexameric molecule with D3 symmetry.
Document Type: Research Article
Publication date: July 1, 2008
More about this publication?
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.