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Literature summary for 4.3.3.7 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)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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]

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

Organism

Organism UniProt Comment Textmining
Sinorhizobium meliloti
-
-
-
Sinorhizobium meliloti L5-30
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Sinorhizobium meliloti

Subunits

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

Synonyms

Synonyms Comment Organism
MosA
-
Sinorhizobium meliloti