CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF BLEOMYCIN-BINDING PROTEIN FROM BLEOMYCIN-PRODUCING STREPTOMYCES-VERTICULLUS

A bleomycin-binding protein (BLMA) produced by bleomycin-producing Str eptomyces verticullus was crystallized in a form suitable for X-ray di ffraction analysis using the vapor-diffusion method. Crystals were gro wn at pH 5.7, in 0.2 M NH4 actate and 0.1 M Na acetate, using 30% PEG 4000 as a precipitant. They belong to the orthorhombic system, with sp ace group P2(1)2(1)2, cell dimensions a = 54.90, b = 67.94, c = 35.60 Angstrom, and one BLMA molecule in the asymmetric unit. The crystals d iffract X-rays well and the diffraction intensity data was collected u p to 1.5 Angstrom resolution with a merging R value of 0.054 at beamli ne 6B of the Photon Factory. The diffraction data set is 94% complete.