Crystallization and preliminary X-ray diffraction data of Mycobacterium tuberculosis FbpC1 (Rv3803c)

RA Wilson, S Rai, William Maughan, L Kremer, Benson Kariuki, Kenneth Harris, T Wagner, Gurdyal Besra, Klaus Futterer

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The heterotrimeric antigen 85 complex (Ag85) is a major component of the cell wall of Mycobacterium tuberculosis and consists of three abundantly secreted proteins ( FbpA, FbpB and FbpC2). These play key roles in the pathogenesis of tuberculosis and in maintaining cell-wall integrity. A homologue of the Ag85 subunits (similar to40% identity) was recently annotated in the M. tuberculosis genome as FbpC1. Unlike the Ag85-complex components, FbpC1 lacks mycolyltransferase activity and its function remains to be established. In order to aid functional characterization, FbpC1 has been crystallized. At room temperature, tetragonal crystals of FbpC1 were obtained belonging to space group P4(1)2(1)2 (unit-cell parameters a = b = 109.9, c = 61.8 Angstrom), yet when frozen the crystals underwent a phase transition to orthorhombic symmetry, space group P2(1)2(1)2(1) (a = 59.9, b = 108.9, c = 109.9 Angstrom). Diffraction data complete to 1.7 Angstrom resolution were recorded at 100 K at the synchrotron.
Original languageEnglish
Pages (from-to)2303-2305
Number of pages3
JournalActa Crystallographica Section D Biological Crystallography
Issue number12
Early online date1 Nov 2003
Publication statusPublished - 27 Nov 2003


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