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Literature summary extracted from

  • Leduc, Y.A.; Phenix, C.P.; Puttick, J.; Nienaber, K.; Palmer, D.R.; Delbaere, L.T.
    Crystallization, preliminary X-ray diffraction and structure solution of MosA, a dihydrodipicolinate synthase from Sinorhizobium meliloti L5-30 (2006), Acta Crystallogr. Sect. F, 62, 49-51.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.3.7 recombinant His-tagged protein is expressed in Escherichia coli BL-21(DE3) Sinorhizobium meliloti

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.3.3.7 crystallization conditions are optimized using vapour diffusion in hanging drops at room temperature. 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 Sinorhizobium meliloti

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.3.7 33000
-
 x * 33000, SDS-PAGE Sinorhizobium meliloti

Organism

EC Number Organism UniProt Comment Textmining
4.3.3.7 Sinorhizobium meliloti
-
-
-
4.3.3.7 Sinorhizobium meliloti L5-30
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.3.7
-
 Sinorhizobium meliloti

Subunits

EC Number Subunits Comment Organism
4.3.3.7 ? x * 33000, SDS-PAGE Sinorhizobium meliloti

Synonyms

EC Number Synonyms Comment Organism
4.3.3.7 MosA
-
 Sinorhizobium meliloti