Crystallization, preliminary X‐ray diffraction and structure solution of MosA, a dihydrodipicolinate synthase from Sinorhizobium meliloti L5‐30

Publisher： John Wiley & Sons Inc

E-ISSN： 1744-3091|62|1|49-51

ISSN： 1744-3091

Source： Acta Crystallographica Section F, Vol.62, Iss.1, 2006-01, pp. : 49-51

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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 Å resolution using synchrotron radiation and belonged to the orthorhombic space group C2221, with unit‐cell parameters a = 69.14, b = 138.87, c = 124.13 Å.

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