EXPRESSION, PURIFICATION, CRYSTALLIZATION, AND PRELIMINARY-X-RAY DIFFRACTION ANALYSIS OF THE HOMODIMERIC BACTERIAL HEMOGLOBIN FROM VITREOSCILLA-STERCORARIA

The recombinant homodimeric hemoglobin from the strictly aerobe gramne gative bacterium Vitreoscilla stercoraria has been expressed in Escher ichia coli, purified to homogeneity, and crystallized by vapor diffusi on techniques, using ammonium sulfate as precipitant. The crystals bel ong to the monoclinic space group P2(1), and diffract to HIGH resoluti on. The unit cell parameters are a = 62.9, b = 42.5, c = 62.2 Angstrom , beta = 106.6 degrees; the asymmetric unit contains the homodimeric h emoglobin, with a volume solvent content of 42%. Proteins 27:154-156 ( C) 1997 Wiley-Liss, Inc.