CRYSTALLIZATION AND PRELIMINARY-X-RAY CRYSTALLOGRAPHIC ANALYSIS OF THE 38-KDA IMMUNODOMINANT ANTIGEN OF MYCOBACTERIUM-TUBERCULOSIS

The 38-kDa lipoprotein is one of the most potent cell surface immunoge ns of Mycobacterium tuberculosis in antibody- and T cell mediated reac tions. Using a pure recombinant form of the protein, we have recently shown that it binds phosphate much like that of the phosphate-binding protein (M(r) = 34.4 kDa) that is localized in the periplasm of Escher ichia coli and is involved as an initial receptor for active transport of phosphate. The purified 38-kDa protein has been crystallized in 2 forms that are suitable for high-resolution structural analyses. One f orm belongs to the monoclinic space group P2(1) with unit cell dimensi ons of a = 67.42 <Angstrom, b = 113.38 Angstrom, c = 42.68 Angstrom, a nd beta = 108.53 degrees. The other is of the orthorhombic space group P2(1)2(1)2 with a = 125.46 Angstrom, b = 72.27 Angstrom, c = 73.43 An gstrom. Both crystal forms diffract to about 2 Angstrom resolution on a fine focus rotating anode.