Published on Aug. 1, 2010 in Acta Crystallogr Sect F Struct Biol Cryst Commun volume 66.
PubMed ID: 20693664
Abstract:
MnmE, an evolutionarily conserved GTPase, is involved in modification of the uridine base (U34) at the wobble position of certain tRNAs. Previous crystal structures of MnmE suggest that it is a dimer with considerable conformational flexibility. To facilitate structural comparisons among MnmE proteins, structural analysis of MnmE from Pseudomonas aeruginosa encoded by the PA5567 gene was initiated. It was overexpressed in Escherichia coli and crystallized at 297 K using a reservoir solution consisting of 100 mM sodium ADA pH 6.5, 12%(w/v) polyethylene glycol 4000, 100 mM lithium sulfate, 2%(v/v) 2-propanol and 2.5 mM dithiothreitol. X-ray diffraction data were collected to 2.69 A resolution. The crystals belonged to the orthorhombic space group C222(1), with unit-cell parameters a=96.74, b=204.66, c=120.90 A. Two monomers were present in the asymmetric unit, resulting in a crystal volume per protein mass (VM) of 2.99 A3 Da(-1) and a solvent content of 58.8%.