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Title: Crystallization, preliminary X-ray diffraction and structure solution of MosA, a dihydrodipicolinate synthase from Sinorhizobium meliloti L5-30. Author: Leduc YA, Phenix CP, Puttick J, Nienaber K, Palmer DR, Delbaere LT. Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2006 Jan 01; 62(Pt 1):49-51. PubMed ID: 16511261. 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.[Abstract] [Full Text] [Related] [New Search]