The subnanometer resolution structure of the glutamate synthase 1.2-mda hexamer by cryoelectron microscopy and its oligomerization behavior in solution

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• who: Magali Cottevieille from the applied to ␤GltSThe secondary structures predicted for ␤GltS were compared with the corresponding ones of DPD calculated by DSSP (44), allowing us to optimize the alignment. This alignment was used with MODELLER, v, (45) to generate homology models by satisfaction of spacial restraints derived from the alignment. The ␣, GltS dimer (Protein Data Bank code, ea, (9)) was submitted to the algorithm "loop" of MODELLER to model the unresolved regions, and , of chains A and B. Only the seven, terminal residues (residues, ) of ␣GltS, absent in the Protein Data Bank file, remain missing . . .
  

   

  

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