An exceptionally stable 1:2 complex [FeL(2)](3-) is formed from the ligand H(3)L and Fe(III). In contrast, the affinity of this ligand for other biometals is relatively small. These properties make H(3)L a highly promising candidate for medical applications (e.g. for the treatment of iron overload).

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The crystal structure of the molecular complex of eglin, a serine proteinase inhibitor from leeches, with subtilisin Carlsberg has been determined at 2.0 A resolution by the molecular replacement method. The complex has been relined by restrained-parameter least-squares. The present crystallographic R factor (=CI ]13,\-]1;1 I/ClF,I) is 0.183. Eglin is a member of the potato inhibitor 1 family, a group of serine proteinase inhibitors lacking disultide bonds. Eglin shows strong structural homology to CL2, a related inhibitor from barley seeds. The structure of subtilisin Carlsberg in this complex is very similar to the known structure of subtilisin novo, despite changes of 84 out of 274 amino acids. Potato inhibitor 1 Serine proteinase Molecular replacement method Hirudo medicinalisCrystallography

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