Crystallization and preliminary X-ray diffraction studies of bleomycin-binding protein encoded on the transposon Tn5
Crystallization and preliminary X-ray diffraction studies of bleomycin-binding protein encoded on the transposon Tn5
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DOI：
10.1107/s0907444999002875
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发表时间：
1999-05-01
期刊：
影响因子：
--
通讯作者：
Sugiyama, M
中科院分区：
文献类型：
--
作者：
Kumagai, T;Maruyama, M;Sugiyama, M
一种博莱霉素结合蛋白，命名为BLMT，编码的转座子Tn 5的结晶，使用气相扩散法在一个适合于X-射线衍射分析的形式。晶体在pH 6.5下在0.1M二甲胂酸钠和0.2M乙酸钙中生长，使用25%PEG 6000作为沉淀剂。它们属于正交晶系，空间群C222（1），晶胞尺寸a = 81.56，B = 85.25，c = 78.91埃，不对称单元中有一个二聚体。在Photon Factory的光束线18 B上收集衍射强度数据，分辨率为2.0埃，合并R值为0.052。衍射数据集已完成91%。
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 C222(1), with unit-cell dimensions a = 81.56, b = 85.25, c = 78.91 Angstrom and one dimer in the asymmetric unit. The diffraction intensity data was collected on beamline 18B of the Photon Factory to 2.0 Angstrom resolution with a merging R value of 0.052. The diffraction data set is 91% complete.