Crystal Structure of Soybean Ferric Leghaemoglobin a Nicotinate at a Resolution of 3.3Ǻ

Abstract

The crystal structure of soybean ferric leghaemoglobin a nicotinate has been solved at 3.3 Å resolution by the multiple isomorphous replacement method. The molecular structure resembles those of other monomeric haemoglobins but is distinguished by the absence of a D helix, an enlargement of the haem pocket, and the possible presence of an additional pathway from the solvent region into the haem pocket.