Publication Abstract from PubMed
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 A and were found to belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell parameters a = 84.5, b = 171.6, c = 184.8 A. Six molecules in the asymmetric unit give a crystal volume per protein mass (V(M)) of 2.97 A (3) 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 D(3) symmetry.
Crystal structure of SCO6571 from Streptomyces coelicolor A3(2).,Begum P, Sakai N, Hayashi T, Gao YG, Tamura T, Watanabe N, Yao M, Tanaka I Protein Pept Lett. 2008;15(7):709-12. PMID:18782066[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
