Premium
Crystallization and preliminary x‐ray crystallographic analysis of the 38‐kda immunodominant antigen of mycobacterium tuberculosis
Author(s) -
Choudhary Abha,
Vyas Meenakshi N.,
Vyas Nand K.,
Chang Zengyi,
Quiocho Florante A.
Publication year - 1994
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560031229
Subject(s) - crystallization , mycobacterium tuberculosis , antigen , crystallography , tuberculosis , x ray , x ray crystallography , chemistry , biology , microbiology and biotechnology , virology , materials science , physics , medicine , diffraction , immunology , pathology , optics , organic chemistry
The 38‐kDa lipoprotein is one of the most potent cell surface immunogens of Mycobacterium tuberculosis in antibody‐and T cell‐mediated reactions. 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 Escherichia 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 form belongs to the monoclinic space group P2 1 with unit cell dimensions of a = 67.42 Å, b = 113.38 Å, c = 42.68 Å, and β = 108.53°. The other is of the orthorhombic space group P2 1 2 1 2 with a = 125.46 Å, b = 72.27 Å, and c = 73.43 Å. Both crystal forms diffract to about 2 Å resolution on a fine focus rotating anode.