Crystallization, preliminary X-ray diffraction and structure solution of MosA, a dihydrodipicolinate synthase from Sinorhizobium meliloti L5-30.
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.
Leduc
Yvonne A
YA
Department of Biochemistry, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E5, Canada.
Phenix
Christopher P
CP
Puttick
Jennifer
J
Nienaber
Kurt
K
Palmer
David R J
DR
Delbaere
Louis T J
LT
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
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D012996:Solutions; D006836:Hydro-Lyases; C020040:4-hydroxy-tetrahydrodipicolinate synthase