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Crystal structure of ferric Aplysia limacina myoglobin at 2.0 Å resolution

1985; Elsevier BV; Volume: 183; Issue: 1 Linguagem: Inglês

10.1016/0022-2836(85)90285-2

1089-8638

Martino Bolognesi, Alessandro Coda, Giuseppina Gatti, Paolo Ascenzi, Maurizio Brunori,

Protein Structure and Dynamics

The three-dimensional structure of ferric myoglobin from the mollusc Aplysia limacina has been refined at 2.0 Å resolution. The crystallographic R factor, calculated at this stage, is 0.194. Despite its high content of apolar residues (both aromatic and aliphatic), Aplysia limacina myoglobin, which contains only one histidine residue (at the proximal position), has a structure that conforms to the common eight-helices globin fold observed in other phyla.