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

Autor:	Leduc, Yvonne A., Phenix, Christopher P., Puttick, Jennifer, Nienaber, Kurt, Palmer, David R. J., Delbaere, Louis T. J.
Předmět:	METHYLTRANSFERASES CRYSTALLIZATION X-ray diffraction ESCHERICHIA coli PYRUVATES RADIATION
Zdroj:	Acta Crystallographica: Section F (Wiley-Blackwell); Jan2006, Vol. 62 Issue 1, p49-51, 3p, 1 Color Photograph, 1 Black and White Photograph, 1 Diagram, 1 Chart
Abstrakt:	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 = 124.13Å. [ABSTRACT FROM AUTHOR]
Databáze:	Complementary Index
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