title: Crystallization, preliminary X-ray diffraction and structure solution of MosA, a dihydrodipicolinate synthase from Sinorhizobium meliloti L5-30.
abstract: The structure of MosA, a dihydrodipicolinate synthase and reported methyltransferase from Sinorhizobium meliloti, has been solved using molecular replacement with Escherichia coli dihydrodipicolinate synthase as the model. A crystal grown in the presence of pyruvate diffracted X-rays to 2.3 A resolution using synchrotron radiation and belonged to the orthorhombic space group C222(1), with unit-cell parameters a = 69.14, b = 138.87, c = 124.13 A.
authors.affiliation: Department of Biochemistry, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E5, Canada.
authors.forename: Yvonne A
authors.initials: YA
authors.lastname: Leduc
authors.forename: Christopher P
authors.initials: CP
authors.lastname: Phenix
authors.forename: Jennifer
authors.initials: J
authors.lastname: Puttick
authors.forename: Kurt
authors.initials: K
authors.lastname: Nienaber
authors.forename: David R J
authors.initials: DR
authors.lastname: Palmer
authors.forename: Louis T J
authors.initials: LT
authors.lastname: Delbaere
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006836:Hydro-Lyases / Q000737:chemistry*; D008027:Light; D011994:Recombinant Proteins / Q000737:chemistry; D012542:Scattering, Radiation; D016962:Sinorhizobium meliloti / Q000201:enzymology*; D012996:Solutions
chemical_list: D001426:Bacterial Proteins; D011994:Recombinant Proteins; D012996:Solutions; D006836:Hydro-Lyases; C020040:4-hydroxy-tetrahydrodipicolinate synthase