Crystallization and preliminary X-ray diffraction studies of bleomycin-binding protein encoded on the transposon Tn5.
A bleomycin-binding protein, designated BLMT, encoded on the transposon Tn5 was crystallized using the vapour-diffusion method in a form suitable for X-ray diffraction analysis. Crystals were grown at pH 6.5 in 0.1 M sodium cacodylate and 0.2 M calcium acetate, using 25% PEG 6000 as a precipitant. They belong to the orthorhombic system, space group C2221, with unit-cell dimensions a = 81.56, b = 85.25, c = 78.91 A and one dimer in the asymmetric unit. The diffraction intensity data were collected on beamline 18B of the Photon Factory to 2.0 A resolution with a merging R value of 0.052. The diffraction data set is 91% complete.
Kumagai
T
T
Institute of Pharmaceutical Sciences, Faculty of Medicine, Hiroshima University, Kasumi 1-2-3, Minami-ku, Hiroshima 734-8551, Japan.
Maruyama
M
M
Matoba
Y
Y
Kawano
Y
Y
Sugiyama
M
M
D000123:Acetyltransferases; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics*; D001761:Bleomycin / Q000378:metabolism*; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004251:DNA Transposable Elements
D001426:Bacterial Proteins; D002352:Carrier Proteins; D004251:DNA Transposable Elements; D001761:Bleomycin; C087954:bleomycin N-acetyltransferase; D000123:Acetyltransferases