Structure Analysis of Macrophage Migration Inhibitory Factor

Abstract

Structure of macrophage migration inhibitory factor has been determined by the method of multiwavelength anomalous diffraction (MAD) with the use of synchrotron data from a crystal of the selenomethionyl protein. The protein contains three methionines in a single polypeptide chain of 114 amino residues. In the analysis, we prepared a series of selenomethionyl proteins by site-directed mutagenesis. The structure was solved using the crystal which contains only one methionine (therefore one Se) per single polypeptide chain.