Abstract

<p><b>A:</b> The A chain is coloured in green and the B chain is shown in blue. The additional disulphide bond is shown by stick representation (yellow). An omit map was calculated by omitting the Sulphur atom of B25C. The resulting difference electron density Fo-Fc map is coloured in orange at σ-level = 3.0. It is clear from the structure that the two monomers are linked by a disulfide bond between the two adjoining B25C. <b>B:</b> Comparison of the B25C structure (blue) with that of the porcine in-sulin (PDB code 1B2E) (grey). The Cα trace shows that the two structures have a high resemblance with minor deviations in Cα positions at residue B21E and B29K.</p

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