Crystallization and preliminary X-ray diffraction studies of bleomycin-binding protein from bleomycin-producing Streptomyces verticillus.
A bleomycin-binding protein (BLMA) produced by bleomycin-producing Streptomyces verticullus was crystallized in a form suitable for X-ray diffraction analysis using the vapor-diffusion method. Crystals were grown 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 space group P21212, cell dimensions a = 54. 90, b = 67.94, c = 35.60 A, and one BLMA molecule in the asymmetric unit. The crystals diffract X-rays well and the diffraction intensity data was collected up to 1.5 A resolution with a merging R value of 0.054 at beamline 6B of the Photon Factory. The diffraction data set is 94% complete.
Institute of Pharmaceutical Sciences, Hiroshima University School of Medicine, Kasumi 1-2-3, Minami-ku, Hiroshima 734, Japan.
T
T
Kumagai
K
K
Muta
Y
Y
Matoba
Y
Y
Kawano
N
N
Kamiya
J
J
Davies
M
M
Sugiyama
D001426:Bacterial Proteins / Q000737:chemistry*; D001761:Bleomycin / Q000096:biosynthesis / Q000737:chemistry*; D003460:Crystallization; D011485:Protein Binding; D013302:Streptomyces / Q000737:chemistry* / Q000378:metabolism; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D001761:Bleomycin